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Enzyme Nomenclature
Information on EC 4.2.1.144 - 3-amino-5-hydroxybenzoate synthase
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4.2.1.144 3-amino-5-hydroxybenzoate synthaseIUBMB Comments
A pyridoxal 5'-phosphate enzyme. The enzyme from the bacterium Amycolatopsis mediterranei participates in the pathway for rifamycin B biosynthesis. The enzyme also functions as a transaminase earlier in the pathway, producing UDP-alpha-D-kanosamine .
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Word Map
- 4.2.1.144
-
ansamycins
- polyketide
- rifamycins
- amycolatopsis
-
starter
-
actinomycete
- mediterranei
- geldanamycin
- synthases
-
endophytic
-
cosmid
- pyridoxal
-
antibiotic-producing
-
naphthalenic
- mitomycin
-
maytansine
-
maytansinoids
-
gene-positive
- hygroscopicus
- erythromycin
-
carbamoyl
-
ansamitocin
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-amino-5-hydroxybenzoic acid synthase
AHBA synthase
rifK
AHBA synthase
-
-
-
-
rifK
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-amino-5-deoxy-3-dehydroshikimate = 3-amino-5-hydroxybenzoate + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
5-amino-5-deoxy-3-dehydroshikimate hydro-lyase (3-amino-5-hydroxybenzoate-forming)
A pyridoxal 5'-phosphate enzyme. The enzyme from the bacterium Amycolatopsis mediterranei participates in the pathway for rifamycin B biosynthesis. The enzyme also functions as a transaminase earlier in the pathway, producing UDP-alpha-D-kanosamine [3].
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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
5-amino-5-deoxy-3-dehydroshikimate
3-amino-5-hydroxybenzoate + H2O
-
-
-
-
?
5-amino-5-deoxy-3-dehydroshikimate
3-amino-5-hydroxybenzoate + H2O
-
-
-
?
5-amino-5-deoxy-3-dehydroshikimate
3-amino-5-hydroxybenzoate + H2O
-
-
-
-
?
5-amino-5-deoxy-3-dehydroshikimate
3-amino-5-hydroxybenzoate + H2O
-
-
-
?
additional information
?
-
no substrates: 5-deoxy-5-amino-3-dehydroquinic acid, 5-deoxy-5-aminoshikimic acid, quinic acid, 3-dehydroquinic acid, or 3-dehydroshikimic acid
-
-
?
additional information
?
-
-
no substrates: 5-deoxy-5-amino-3-dehydroquinic acid, 5-deoxy-5-aminoshikimic acid, quinic acid, 3-dehydroquinic acid, or 3-dehydroshikimic acid
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
enzyme is a dimer containing one molecule of pyridoxal phosphate per subunit. The enzyme-bound pyridoxal phosphate forms a SchiffĆ¢ĀĀs base with the amino group of 5-deoxy-5-amino-3-dehydroshikimic acid and catalyzes both an alpha,beta-dehydration and a stereospecific 1,4-enolization of the substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-deoxy-D-arabinoheptulosonic acid 7-phosphate
1 mM, 40-50% activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
enzyme is part of the aminoshikimate pathway of formation of 3-amino-5-hydroxybenzoic acid, the precursor of ansamycin and other antibiotics. Nitrogenous precursor Kanosamine is phosphorylated and converted into 1-deoxy-1-imino-erythrose 4-phosphate, the substrate for the formation of 3,4-dideoxy-4-amino-D-arabino-seduheptulosonic acid 7-phosphate. This is converted via 5-deoxy-5-aminodehydroquinic acid and 5-deoxy-5-aminodehydroshikimic acid into 3-amino-5-hydroxybenzoic acid. 3-amino-5-hydroxybenzoic acid synthase seems to have two catalytic functions. As a homodimer, it catalyzes the last reaction in the pathway, the aromatization of 5-deoxy-5-aminodehydroshikimic acid, and at the beginning of the pathway in a complex with the oxidoreductase RifL it catalyzes the transamination of UDP-3-keto-D-glucose
physiological function
involved in rifamycin B biosynthesis. Starter enzyme for the assembly of the antibiotics' polyketide backbone
physiological function
-
involved in rifamycin B biosynthesis. Starter enzyme for the assembly of the antibiotics' polyketide backbone
-
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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). RIFK_AMYMS
Amycolatopsis mediterranei (strain S699)
388
0
42211
Swiss-Prot
-
A0A1V5SS93_9BACT
432
0
48391
TrEMBL
-
A0A238KZ34_9RHOB
385
0
42118
TrEMBL
-
A0A1V5FGX8_9BACT
432
0
48280
TrEMBL
-
A0A518LB71_9BACT
355
0
38629
TrEMBL
-
A0A1V5Z535_9BACT
259
0
28533
TrEMBL
-
A0A1V5YYJ4_9BACT
398
0
43834
TrEMBL
-
A0A1V6F1E1_9BACT
440
0
48412
TrEMBL
-
A0A7T1ALH3_9BACT
432
0
48189
TrEMBL
-
A0A1V5YQA5_9BACT
365
0
40994
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with pyridoxal 5'-phosphate and with pyridoxal 5'-phosphate and inhibitor gabaculine. The overall fold of is similar to that of the aspartate aminotransferase family of PLP-dependent enzymes, with a large domain containing a seven-stranded beta-sheet surrounded by alpha-helices and a smaller domain consisting of a four-stranded antiparallel beta-sheet and four alpha-helices. The uninhibited form of the enzyme shows the cofactor covalently linked to residue Lys188 in an internal aldimine linkage. On binding the inhibitor, gabaculine, the internal aldimine linkage is broken, and a covalent bond is observed between the cofactor and inhibitor. The active site is composed of residues from two subunits, indicating that the enzyme is active as a dimer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eads, J.C.; Beeby, M.; Scapin, G.; Yu, T.W.; Floss, H.G.
Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase
Biochemistry
38
9840-9849
1999
Amycolatopsis mediterranei (O52552), Amycolatopsis mediterranei, Amycolatopsis mediterranei S699 (O52552)
brenda
Wu, L.; Liu, A.; Ma, C.; Han, F.; Zhang, H.; Gao, Q.; Wang, Y.
Cloning of 3-amino-5-hydroxybenzoic acid (AHBA) synthase gene from Streptomyces sp. 4353 and its expression in E. coli
Chin. J. Antibiot.
34
24-29
2009
Streptomyces sp. (B3VD87), Streptomyces sp. 4353 (B3VD87)
-
brenda
Floss, H.G.; Yu, T.W.; Arakawa, K.
The biosynthesis of 3-amino-5-hydroxybenzoic acid (AHBA), the precursor of mC7N units in ansamycin and mitomycin antibiotics: a review
J. Antibiot.
64
35-44
2011
Amycolatopsis mediterranei
brenda
Kim, C.G.; Yu, T.W.; Fryhle, C.B.; Handa, S.; Floss, H.G.
3-Amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics
J. Biol. Chem.
273
6030-6040
1998
Amycolatopsis mediterranei (O52552), Amycolatopsis mediterranei
brenda
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