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Information on EC 3.1.21.4 - type II site-specific deoxyribonuclease and Organism(s) Haemophilus influenzae and UniProt Accession P20588
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3.1.21.4 type II site-specific deoxyribonucleaseSpecify your search results
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- 3.1.21.4
- endonucleases
- phage
- lambda
- agarose
- strand
- rrna
- bacteriophage
-
pcr-rflp
- viruses
-
serotype
-
pulsed-field
-
single-stranded
-
spacers
-
cosmid
-
amplicons
- adenovirus
-
outbreak
- simplex
- herpes
- mtdnas
- cytosine
- duplex
-
serological
-
pcr-based
-
nested
-
epstein-barr
- cpg
-
caucasian
-
methylase
-
reaction-restriction
- herpesvirus
- virion
- satellite
- tetracycline
-
nosocomial
-
32p-labeled
-
proviral
- beta-globin
-
simian
- ethidium
- globin
- ampicillin
-
discriminatory
-
dna-dna
-
unmethylated
-
supercoiled
- serogroups
-
biotype
-
subfragment
- analysis
- biotechnology
- beta-thalassemia
- molecular biology
The taxonomic range for the selected organisms is: Haemophilus influenzae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Synonyms
restriction enzyme, restriction endonuclease, ecori, hindiii, bamhi, pvuii, haeiii, hpaii, bglii, ecorv, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DNA restriction endonuclease
-
-
-
-
DNA restriction enzyme
-
-
-
-
EC 3.1.23
-
-
-
-
EC 3.1.24
-
-
-
-
Endonuclease AbrI
-
-
-
-
Endonuclease AccI
-
-
-
-
Endonuclease AgeI
-
-
-
-
Endonuclease ApaLI
-
-
-
-
Endonuclease AvaI
-
-
-
-
Endonuclease BamHI
-
-
-
-
Endonuclease BanI
-
-
-
-
Endonuclease BglI
-
-
-
-
Endonuclease BglII
-
-
-
-
Endonuclease BsoBI
-
-
-
-
Endonuclease Bsp6I
-
-
-
-
Endonuclease BstVI
-
-
-
-
Endonuclease BsuBI
-
-
-
-
Endonuclease BsuFI
-
-
-
-
Endonuclease BsuRI
-
-
-
-
Endonuclease CeqI
-
-
-
-
Endonuclease Cfr10I
-
-
-
-
Endonuclease Cfr9I
-
-
-
-
Endonuclease CfrBI
-
-
-
-
Endonuclease CviAII
-
-
-
-
Endonuclease CviJI
-
-
-
-
Endonuclease DdeI
-
-
-
-
Endonuclease DpnI
-
-
-
-
Endonuclease DpnII
-
-
-
-
Endonuclease Eco47I
-
-
-
-
Endonuclease Eco47II
-
-
-
-
Endonuclease EcoRI
-
-
-
-
Endonuclease EcoRII
-
-
-
-
Endonuclease EcoRV
-
-
-
-
Endonuclease FokI
-
-
-
-
Endonuclease HaeII
-
-
-
-
Endonuclease HaeIII
-
-
-
-
Endonuclease HgAI
-
-
-
-
Endonuclease HgiBI
-
-
-
-
Endonuclease HgiCI
-
-
-
-
Endonuclease HgiCII
-
-
-
-
Endonuclease HgiDI
-
-
-
-
Endonuclease HgiEI
-
-
-
-
Endonuclease HgiGI
-
-
-
-
Endonuclease HhaII
-
-
-
-
Endonuclease HincII
-
-
-
-
Endonuclease HindII
-
-
-
-
Endonuclease HindIII
-
-
-
-
Endonuclease HindVP
-
-
-
-
Endonuclease HinfI
-
-
-
-
Endonuclease HpaI
-
-
-
-
Endonuclease HpaII
-
-
-
-
Endonuclease HphI
-
-
-
-
Endonuclease KpnI
-
-
-
-
Endonuclease LlaDCHI
-
-
-
-
Endonuclease MamI
-
-
-
-
Endonuclease MboI
-
-
-
-
Endonuclease MboII
-
-
-
-
Endonuclease MjaI
-
-
-
-
Endonuclease MjaII
-
-
-
-
Endonuclease MjaIII
-
-
-
-
Endonuclease MjaIV
-
-
-
-
Endonuclease MjaV
-
-
-
-
Endonuclease MjaVIP
-
-
-
-
Endonuclease MspI
-
-
-
-
Endonuclease MthTI
-
-
-
-
Endonuclease MthZI
-
-
-
-
Endonuclease MunI
-
-
-
-
Endonuclease MwoI
-
-
-
-
Endonuclease NaeI
-
-
-
-
Endonuclease NgoBI
-
-
-
-
Endonuclease NgoBV
-
-
-
-
Endonuclease NgoFVII
-
-
-
-
Endonuclease NgoMIV
-
-
-
-
Endonuclease NgoPII
-
-
-
-
Endonuclease NlaIII
-
-
-
-
Endonuclease NlaIV
-
-
-
-
Endonuclease NmeDIP
-
-
-
-
Endonuclease NspV
-
-
-
-
Endonuclease PaeR7I
-
-
-
-
Endonuclease PstI
-
-
-
-
Endonuclease PvuI
-
-
-
-
Endonuclease PvuII
-
-
-
-
Endonuclease RsrI
-
-
-
-
Endonuclease SacI
-
-
-
-
Endonuclease SalI
-
-
-
-
Endonuclease Sau3AI
-
-
-
-
Endonuclease Sau96I
-
-
-
-
Endonuclease ScaI
-
-
-
-
Endonuclease ScrFI
-
-
-
-
Endonuclease SfiI
-
-
-
-
Endonuclease SinI
-
-
-
-
Endonuclease SmaI
-
-
-
-
Endonuclease SsoII
-
-
-
-
Endonuclease StsI
-
-
-
-
Endonuclease TaqI
-
-
-
-
Endonuclease TthHB8I
-
-
-
-
Endonuclease XamI
-
-
-
-
Endonuclease XcyI
-
-
-
-
HincII
HindIII
LlaII
-
-
-
-
nuclease, deoxyribonucleic restriction endo-
-
-
-
-
nuclease, restriction endodeoxyribo-
-
-
-
-
R.AbrI
-
-
-
-
R.AccI
-
-
-
-
R.AgeI
-
-
-
-
R.ApaLI
-
-
-
-
R.AvaI
-
-
-
-
R.BamHI
-
-
-
-
R.BanI
-
-
-
-
R.BglI
-
-
-
-
R.BglII
-
-
-
-
R.BsoBI
-
-
-
-
R.Bsp6I
-
-
-
-
R.BstVI
-
-
-
-
R.BsuBI
-
-
-
-
R.BsuRI
-
-
-
-
R.CeqI
-
-
-
-
R.Cfr10I
-
-
-
-
R.Cfr9I
-
-
-
-
R.CfrBI
-
-
-
-
R.CviAII
-
-
-
-
R.CviJI
-
-
-
-
R.DdeI
-
-
-
-
R.DpnI
-
-
-
-
R.DpnII
-
-
-
-
R.Eco47I
-
-
-
-
R.Eco47II
-
-
-
-
R.EcoRI
-
-
-
-
R.EcoRII
-
-
-
-
R.EcoRV
-
-
-
-
R.FokI
-
-
-
-
R.HaeII
-
-
-
-
R.HaeIII
-
-
-
-
R.HgAI
-
-
-
-
R.HgiBI
-
-
-
-
R.HgiCI
-
-
-
-
R.HgiCII
-
-
-
-
R.HgiDI
-
-
-
-
R.HgiEI
-
-
-
-
R.HgiGI
-
-
-
-
R.HhaII
-
-
-
-
R.HincII
-
-
-
-
R.HindII
-
-
-
-
R.HindIII
-
-
-
-
R.HindVP
-
-
-
-
R.HinfI
-
-
-
-
R.HpaI
-
-
-
-
R.HpaII
-
-
-
-
R.HphI
-
-
-
-
R.KpnI
-
-
-
-
R.LlaDCHI
-
-
-
-
R.MamI
-
-
-
-
R.MboI
-
-
-
-
R.MboII
-
-
-
-
R.MjaI
-
-
-
-
R.MjaII
-
-
-
-
R.MjaIII
-
-
-
-
R.MjaIV
-
-
-
-
R.MjaV
-
-
-
-
R.MjaVIP
-
-
-
-
R.MspI
-
-
-
-
R.MthTI
-
-
-
-
R.MthZI
-
-
-
-
R.MunI
-
-
-
-
R.MwoI
-
-
-
-
R.NaeI
-
-
-
-
R.NgoBI
-
-
-
-
R.NgoBV
-
-
-
-
R.NgoFVII
-
-
-
-
R.NgoI
-
-
-
-
R.NgoMIV
-
-
-
-
R.NgoPII
-
-
-
-
R.NgoV
-
-
-
-
R.NgoVII
-
-
-
-
R.NlaIII
-
-
-
-
R.NlaIV
-
-
-
-
R.NmeDIP
-
-
-
-
R.NspV
-
-
-
-
R.PaeR7I
-
-
-
-
R.PstI
-
-
-
-
R.PvuI
-
-
-
-
R.PvuII
-
-
-
-
R.RsrI
-
-
-
-
R.SacI
-
-
-
-
R.SalI
-
-
-
-
R.Sau3AI
-
-
-
-
R.Sau96I
-
-
-
-
R.ScaI
-
-
-
-
R.ScrFI
-
-
-
-
R.SfiI
-
-
-
-
R.SinI
-
-
-
-
R.SmaI
-
-
-
-
R.SsoII
-
-
-
-
R.StsI
-
-
-
-
R.TaqI
-
-
-
-
R.TthHB8I
-
-
-
-
R.XamI
-
-
-
-
R.XcyI
-
-
-
-
restriction endodeoxyribonuclease
-
-
-
-
restriction endonuclease
-
-
-
-
restriction enzyme
-
-
-
-
type II restriction enzyme
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9075-08-5
not distinguished from EC 3.1.21.5
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
-
-
?
DNA + H2O
?
-
sequence-specific endonucleolytic digestion of infecting DNA
-
-
?
DNA containing 5-fluoro-dC + H2O
?
perfectly hydrolyzes the DNA containing F5dC
-
-
?
DNA containing 5-fluoro-dU + H2O
?
perfectly hydrolyzes the DNA containing F5dU
-
-
?
DNA containing 5-methyl-dC + H2O
?
hydrolyzes the DNA containing F5dC
-
-
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
cleavage by HindII is blunt, producing fragments with flush ends
-
-
?
additional information
?
-
-
restriction endonuclease activity and modification methylase activity occur as separate proteins
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
HinP1I recognizes and cleaves a palindromic tetranucleotide sequence (G-/-CGC) in double-stranded DNA, producing 2 nt 5' overhanging ends
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
recognition sequence of HincII: GTYRAC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
recognition sequence of HindIII: AAGCTT. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
-
sequence-specific endonucleolytic digestion of infecting DNA
-
-
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
cleavage by HindII is blunt, producing fragments with flush ends
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 28000, the enzyme can form a dimer or a higher order molecule weight complex at high protein concentrations
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of mutant enzyme Q138F bound to GTTAAC, GTCGAC both with and without Ca2+, as well as the structure of the wild-type HincII bound to GTTAAC
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q138F
mutation results in a change in the sequence specificity at the center two base pairs of the cognate recognition site. Alteration in preference of HicII for cutting, but not binding, the three cognate sites differening in the center two base pairs.The Q138F HincII/DNA crystal structures show conformational changes in the protein, bound DNA, and at the protein-DNA interface
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the complete restriction-modification system in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roberts, R.J.
Restriction enzymes and their isoschizomers
Nucleic Acids Res.
18
2331-2365
1990
Acetobacter aceti, Gluconobacter oxydans, Acetobacter pasteurianus, Acinetobacter lwoffii, Streptomyces phaeochromogenes, Thalassobius gelatinovorus, Anabaena cylindrica, Dolichospermum flos-aquae, Anabaena subcylindrica, Trichormus variabilis, Synechocystis sp., Aphanothece halophytica, Cellulosimicrobium cellulans, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Brevibacillus brevis, [Bacillus] caldolyticus, Bacillus cereus, Weizmannia coagulans, Bacillus subtilis, Bacillus pumilus, Lysinibacillus sphaericus, uncultured bacterium, Bifidobacterium longum subsp. infantis, Curtobacterium albidum, Caryophanon latum, Chloroflexus aurantiacus, Chromobacterium violaceum, Citrobacter freundii, Dactylococcus salina, Deinococcus radiodurans, Deinococcus radiophilus, Desulfovibrio desulfuricans, Streptococcus pneumoniae, Escherichia coli, Enterococcus faecalis, Eucapsis sp., Flavobacterium aquatile, Chryseobacterium indologenes, Planomicrobium okeanokoites, Thermus thermophilus, Frankia sp., Fusobacterium nucleatum, Haemophilus aegyptius, Avibacterium paragallinarum, Haemophilus haemolyticus, Haemophilus influenzae, Haemophilus parahaemolyticus, Haemophilus parainfluenzae, Herpetosiphon aurantiacus, Klebsiella pneumoniae, Methanothermobacter wolfeii, Methanococcus aeolicus, Methylophilus methylotrophus, Psychrobacter urativorans, Micrococcus luteus, Micrococcus lylae, Staphylococcus aureus, Microcoleus sp., Moraxella bovis, Moraxella nonliquefaciens, Mycoplasmopsis fermentans, Bergeriella denitrificans, Neisseria lactamica, Neisseria mucosa heidelbergensis, Lentzea aerocolonigenes, Nocardia argentinensis, Gordonia rubripertincta, Nocardia otitidiscaviarum, Rhodococcus ruber, Nostoc sp., Plesiomonas shigelloides, Proteus vulgaris, Pseudomonas sp., Pseudomonas putida, Pseudomonas fluorescens, Paucimonas lemoignei, Stenotrophomonas maltophilia, Pseudomonas stutzeri, Rhizobium leguminosarum, Cereibacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhi, Serratia marcescens, Sphaerotilus natans, Sphaerotilus sp., Arthrospira platensis, Streptomyces achromogenes, Lactococcus cremoris, Enterococcus durans, Streptomyces albus, Streptomyces caespitosus, Streptomyces fimbriatus, Thermus aquaticus, Thermus filiformis, Thermus sp., Vibrio sp., Xanthomonas campestris pv. badrii, Xanthomonas campestris, Xanthomonas phaseoli pv. manihotis, Xanthomonas vasicola, Xanthomonas citri pv. malvacearum, Acetobacter pasteurianus ApaLI
Wells, R.D.; Klein, R.D.; Singleton, C.K.
Type II restriction enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
14
157-191
1981
Trichormus variabilis, Cellulosimicrobium cellulans, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, [Bacillus] caldolyticus, Bacillus subtilis, Lysinibacillus sphaericus, Desulfovibrio desulfuricans, Streptococcus pneumoniae, Escherichia coli, Enterococcus faecalis, Thermus thermophilus, Fusobacterium nucleatum, Haemophilus aegyptius, Avibacterium paragallinarum, Haemophilus haemolyticus, Haemophilus influenzae, Haemophilus parahaemolyticus, Haemophilus parainfluenzae, Herpetosiphon aurantiacus, Staphylococcus aureus, Moraxella bovis, Providencia stuartii, Cereibacter sphaeroides, Serratia marcescens, Streptomyces achromogenes, Streptomyces albus, Xanthomonas campestris pv. badrii, Xanthomonas vasicola, Xanthomonas citri pv. malvacearum, Staphylococcus aureus Sau96I
-
Wilson, G.G.
Type II restriction-modification systems
Trends Genet.
4
314-318
1988
Dolichospermum flos-aquae, Trichormus variabilis, Bacillus amyloliquefaciens, Bacillus subtilis, Desulfovibrio desulfuricans, Streptococcus pneumoniae, Escherichia coli, Planomicrobium okeanokoites, Haemophilus aegyptius, Haemophilus haemolyticus, Haemophilus influenzae, Herpetosiphon aurantiacus, Methanothermobacter wolfeii, Proteus vulgaris, Providencia stuartii, Streptomyces albus, Thermus aquaticus, Xanthomonas campestris pv. badrii
Glenn, T.C.; Waller, D.R.; Braun, M.J.
Increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
Biotechniques
17
1086-1090
1994
Acetobacter pasteurianus, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Caryophanon latum, Escherichia coli, Haemophilus influenzae, Klebsiella pneumoniae, Nocardia otitidiscaviarum, Pseudomonas sp., Serratia marcescens, Streptomyces achromogenes, Xanthomonas campestris pv. badrii, Acetobacter pasteurianus ApaI, Geobacillus stearothermophilus BstXI, Geobacillus stearothermophilus BstZI
Joshi, H.K.; Etzkorn, C.; Chatwell, L.; Bitinaite, J.; Horton, N.C.
Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism
J. Biol. Chem.
281
23852-23869
2006
Haemophilus influenzae (P17743)
Yang, Z.; Horton, J.R.; Maunus, R.; Wilson, G.G.; Roberts, R.J.; Cheng, X.
Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI
Nucleic Acids Res.
33
1892-1901
2005
Haemophilus influenzae
Nikolajewa, S.; Beyer, A.; Friedel, M.; Hollunder, J.; Wilhelm, T.
Common patterns in type II restriction enzyme binding sites
Nucleic Acids Res.
33
2726-2733
2005
Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Citrobacter freundii, Escherichia coli, Planomicrobium okeanokoites, Haemophilus influenzae, Moraxella sp., Mycoplasma sp., Neisseria gonorrhoeae, Lentzea aerocolonigenes, Proteus vulgaris
Orlowski, J.; Bujnicki, J.M.
Structural and evolutionary classification of type II restriction enzymes based on theoretical and experimental analyses
Nucleic Acids Res.
36
3552-3569
2008
Trichormus variabilis, Caryophanon latum, Helicobacter pylori, Helicobacter pylori (Q9ZLF0), Helicobacter pylori (Q9ZN14), Methylococcus capsulatus, Pyrococcus horikoshii, Staphylococcus hominis, Sulfolobus acidocaldarius, Thermus aquaticus, Corynebacterium striatum, Streptomyces achromogenes (O31074), Haemophilus parahaemolyticus (P00643), Serratia marcescens (P14229), Haemophilus influenzae (P20588), Staphylococcus aureus (P23736), Herpetosiphon aurantiacus (P25260), Nostoc sp. (P35677), Citrobacter freundii (Q04852), Sporosarcina sp. (Q194N8), Micrococcus sp. (Q2I0D9), Methanocaldococcus jannaschii (Q58723), Methanocaldococcus jannaschii (Q58895), Moraxella sp. (Q6S4U8), Sphaerotilus natans (Q6SA25), Cereibacter sphaeroides (Q6SA27), Geobacillus stearothermophilus (Q8L3A5), Lactococcus lactis (Q93K18), Thermus filiformis (Q9F8S3), Thalassobius gelatinovorus (Q9KHV6), Xanthomonas vasicola (Q9KVZ7), Neisseria meningitidis (Q9RLM3), Corynebacterium striatum M82B, Moraxella sp. A1 (Q6S4U8), Micrococcus sp. NEB 446 (Q2I0D9)
Pingoud, A.; Wilson, G.G.; Wende, W.
Type II restriction endonucleases-a historical perspective and more
Nucleic Acids Res.
42
7489-7527
2014
Escherichia coli, Haemophilus influenzae
Olszewska, A.; Dadova, J.; Mackova, M.; Hocek, M.
Cleavage of DNA containing 5-fluorocytosine or 5-fluorouracil by type II restriction endonucleases
Bioorg. Med. Chem.
23
6885-6890
2015
Dolichospermum flos-aquae (E3VX87), Streptomyces caespitosus (O52691), Acetobacter pasteurianus (O52703), Gordonia rubripertincta (O85489), Pyrococcus sp. GI-H (O93646), Providencia stuartii (P00640), Escherichia coli (P00642), Proteus hauseri (P23657), Bacillus amyloliquefaciens (P23940), Klebsiella pneumoniae (P25237), Haemophilus influenzae (P43870), Bacillus subtilis (Q45488), Acidithiobacillus ferrooxidans (Q4GZN8), Fuscovulum blasticum (Q6SA27), Dolichospermum flos-aquae CCAP 1403/13F (E3VX87), Haemophilus influenzae ATCC 51907 (P43870)
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