Sequence of ERYA2_SACER

EC Number:2.3.1.B32

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
[acyl-carrier-protein] S-methylmalonyltransferase
Q03132
Saccharopolyspora erythraea
3567
374421
Reaction
methylmalonyl-CoA + an [acyl-carrier protein] = CoA + a methylmalonyl-[acyl-carrier protein]
Other sequences found for EC No. 2.3.1.B32

EC Number:2.3.1.94

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
6-deoxyerythronolide-B synthase
Q03132
Saccharopolyspora erythraea
3567
374421
Reaction
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
Other sequences found for EC No. 2.3.1.94

EC Number:4.2.1.61

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
Q03132
Saccharopolyspora erythraea
3567
374421
Reaction
Other sequences found for EC No. 4.2.1.61

General information:

Sequence
show sequence in fasta format
   0 MTDSEKVAEY LRRATLDLRA ARQRIRELES DPIAIVSMAC RLPGGVNTPQ RLWELLREGG
  60 ETLSGFPTDR GWDLARLHHP DPDNPGTSYV DKGGFLDDAA GFDAEFFGVS PREAAAMDPQ
 120 QRLLLETSWE LVENAGIDPH SLRGTATGVF LGVAKFGYGE DTAAAEDVEG YSVTGVAPAV
 180 ASGRISYTMG LEGPSISVDT ACSSSLVALH LAVESLRKGE SSMAVVGGAA VMATPGVFVD
 240 FSRQRALAAD GRSKAFGAGA DGFGFSEGVT LVLLERLSEA RRNGHEVLAV VRGSALNQDG
 300 ASNGLSAPSG PAQRRVIRQA LESCGLEPGD VDAVEAHGTG TALGDPIEAN ALLDTYGRDR
 360 DADRPLWLGS VKSNIGHTQA AAGVTGLLKV VLALRNGELP ATLHVEEPTP HVDWSSGGVA
 420 LLAGNQPWRR GERTRRARVS AFGISGTNAH VIVEEAPERE HRETTAHDGR PVPLVVSART
 480 TAALRAQAAQ IAELLERPDA DLAGVGLGLA TTRARHEHRA AVVASTREEA VRGLREIAAG
 540 AATADAVVEG VTEVDGRNVV FLFPGQGSQW AGMGAELLSS SPVFAGKIRA CDESMAPMQD
 600 WKVSDVLRQA PGAPGLDRVD VVQPVLFAVM VSLAELWRSY GVEPAAVVGH SQGEIAAAHV
 660 AGALTLEDAA KLVVGRSRLM RSLSGEGGMA AVALGEAAVR ERLRPWQDRL SVAAVNGPRS
 720 VVVSGEPGAL RAFSEDCAAE GIRVRDIDVD YASHSPQIER VREELLETTG DIAPRPARVT
 780 FHSTVESRSM DGTELDARYW YRNLRETVRF ADAVTRLAES GYDAFIEVSP HPVVVQAVEE
 840 AVEEADGAED AVVVGSLHRD GGDLSAFLRS MATAHVSGVD IRWDVALPGA APFALPTYPF
 900 QRKRYWLQPA APAAASDELA YRVSWTPIEK PESGNLDGDW LVVTPLISPE WTEMLCEAIN
 960 ANGGRALRCE VDTSASRTEM AQAVAQAGTG FRGVLSLLSS DESACRPGVP AGAVGLLTLV
1020 QALGDAGVDA PVWCLTQGAV RTPADDDLAR PAQTTAHGFA QVAGLELPGR WGGVVDLPES
1080 VDDAALRLLV AVLRGGGRAE DHLAVRDGRL HGRRVVRASL PQSGSRSWTP HGTVLVTGAA
1140 SPVGDQLVRW LADRGAERLV LAGACPGDDL LAAVEEAGAS AVVCAQDAAA LREALGDEPV
1200 TALVHAGTLT NFGSISEVAP EEFAETIAAK TALLAVLDEV LGDRAVEREV YCSSVAGIWG
1260 GAGMAAYAAG SAYLDALAEH HRARGRSCTS VAWTPWALPG GAVDDGYLRE RGLRSLSADR
1320 AMRTWERVLA AGPVSVAVAD VDWPVLSEGF AATRPTALFA ELAGRGGQAE AEPDSGPTGE
1380 PAQRLAGLSP DEQQENLLEL VANAVAEVLG HESAAEINVR RAFSELGLDS LNAMALRKRL
1440 SASTGLRLPA SLVFDHPTVT ALAQHLRARL VGDADQAAVR VVGAADESEP IAIVGIGCRF
1500 PGGIGSPEQL WRVLAEGANL TTGFPADRGW DIGRLYHPDP DNPGTSYVDK GGFLTDAADF
1560 DPGFFGITPR EALAMDPQQR LMLETAWEAV ERAGIDPDAL RGTDTGVFVG MNGQSYMQLL
1620 AGEAERVDGY QGLGNSASVL SGRIAYTFGW EGPALTVDTA CSSSLVGIHL AMQALRRGEC
1680 SLALAGGVTV MSDPYTFVDF STQRGLASDG RCKAFSARAD GFALSEGVAA LVLEPLSRAR
1740 ANGHQVLAVL RGSAVNQDGA SNGLAAPNGP SQERVIRQAL AASGVPAADV DVVEAHGTGT
1800 ELGDPIEAGA LIATYGQDRD RPLRLGSVKT NIGHTQAAAG AAGVIKVVLA MRHGMLPRSL
1860 HADELSPHID WESGAVEVLR EEVPWPAGER PRRAGVSSFG VSGTNAHVIV EEAPAEQEAA
1920 RTERGPLPFV LSGRSEAVVA AQARALAEHL RDTPELGLTD AAWTLATGRA RFDVRAAVLG
1980 DDRAGVCAEL DALAEGRPSA DAVAPVTSAP RKPVLVFPGQ GAQWVGMARD LLESSEVFAE
2040 SMSRCAEALS PHTDWKLLDV VRGDGGPDPH ERVDVLQPVL FSIMVSLAEL WRAHGVTPAA
2100 VVGHSQGEIA AAHVAGALSL EAAAKVVALR SQVLRELDDQ GGMVSVGASR DELETVLARW
2160 DGRVAVAAVN GPGTSVVAGP TAELDEFFAE AEAREMKPRR IAVRYASHSP EVARIEDRLA
2220 AELGTITAVR GSVPLHSTVT GEVIDTSAMD ASYWYRNLRR PVLFEQAVRG LVEQGFDTFV
2280 EVSPHPVLLM AVEETAEHAG AEVTCVPTLR REQSGPHEFL RNLLRAHVHG VGADLRPAVA
2340 GGRPAELPTY PFEHQRFWPR PHRPADVSAL GVRGAEHPLL LAAVDVPGHG GAVFTGRLST
2400 DEQPWLAEHV VGGRTLVPGS VLVDLALAAG EDVGLPVLEE LVLQRPLVLA GAGALLRMSV
2460 GAPDESGRRT IDVHAAEDVA DLADAQWSQH ATGTLAQGVA AGPRDTEQWP PEDAVRIPLD
2520 DHYDGLAEQG YEYGPSFQAL RAAWRKDDSV YAEVSIAADE EGYAFHPVLL DAVAQTLSLG
2580 ALGEPGGGKL PFAWNTVTLH ASGATSVRVV ATPAGADAMA LRVTDPAGHL VATVDSLVVR
2640 STGEKWEQPE PRGGEGELHA LDWGRLAEPG STGRVVAADA SDLDAVLRSG EPEPDAVLVR
2700 YEPEGDDPRA AARHGVLWAA ALVRRWLEQE ELPGATLVIA TSGAVTVSDD DSVPEPGAAA
2760 MWGVIRCAQA ESPDRFVLLD TDAEPGMLPA VPDNPQLALR GDDVFVPRLS PLAPSALTLP
2820 AGTQRLVPGD GAIDSVAFEP APDVEQPLRA GEVRVDVRAT GVNFRDVLLA LGMYPQKADM
2880 GTEAAGVVTA VGPDVDAFAP GDRVLGLFQG AFAPIAVTDH RLLARVPDGW SDADAAAVPI
2940 AYTTAHYALH DLAGLRAGQS VLIHAAAGGV GMAAVALARR AGAEVLATAG PAKHGTLRAL
3000 GLDDEHIASS RETGFARKFR ERTGGRGVDV VLNSLTGELL DESADLLAED GVFVEMGKTD
3060 LRDAGDFRGR YAPFDLGEAG DDRLGEILRE VVGLLGAGEL DRLPVSAWEL GSAPAALQHM
3120 SRGRHVGKLV LTQPAPVDPD GTVLITGGTG TLGRLLARHL VTEHGVRHLL LVSRRGADAP
3180 GSDELRAEIE DLGASAEIAA CDTADRDALS ALLDGLPRPL TGVVHAAGVL ADGLVTSIDE
3240 PAVEQVLRAK VDAAWNLHEL TANTGLSFFV LFSSAASVLA GPGQGVYAAA NESLNALAAL
3300 RRTRGLPAKA LGWGLWAQAS EMTSGLGDRI ARTGVAALPT ERALALFDSA LRRGGEVVFP
3360 LSINRSALRR AEFVPEVLRG MVRAKLRAAG QAEAAGPNVV DRLAGRSESD QVAGLAELVR
3420 SHAAAVSGYG SADQLPERKA FKDLGFDSLA AVELRNRLGT ATGVRLPSTL VFDHPTPLAV
3480 AEHLRDRLFA ASPAVDIGDR LDELEKALEA LSAEDGHDDV GQRLESLLRR WNSRRADAPS
3540 TSAISEDASD DELFSMLDQR FGGGEDL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
159041
Donadio S.,Staver M.J.,McAlpine J.B.,Swanson S.J.,Katz L.
Modular organization of genes required for complex polyketide biosynthesis.
Science
252
675-679
1991
159042
Bevitt D.J.,Cortes J.,Haydock S.F.,Leadlay P.F.
6-deoxyerythronolide-B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme.
Eur. J. Biochem.
204
39-49
1992
159043
Caffrey P.,Bevitt D.J.,Staunton J.,Leadlay P.F.
Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea.
FEBS Lett.
304
225-228
1992
159044
Khosla C.,Tang Y.,Chen A.Y.,Schnarr N.A.,Cane D.E.
Structure and mechanism of the 6-deoxyerythronolide B synthase.
Annu. Rev. Biochem.
76
195-221
2007
159045
Kwan D.H.,Sun Y.,Schulz F.,Hong H.,Popovic B.,Sim-Stark J.C.,Haydock S.F.,Leadlay P.F.
Prediction and manipulation of the stereochemistry of enoylreduction in modular polyketide synthases.
Chem. Biol.
15
1231-1240
2008
159046
Zhang H.,Wang Y.,Wu J.,Skalina K.,Pfeifer B.A.
Complete biosynthesis of erythromycin A and designed analogs using E. coli as a heterologous host.
Chem. Biol.
17
1232-1240
2010
159047
Zheng J.,Keatinge-Clay A.T.
Structural and functional analysis of C2-type ketoreductases from modular polyketide synthases.
J. Mol. Biol.
410
105-117
2011
159048
Broadhurst R.W.,Nietlispach D.,Wheatcroft M.P.,Leadlay P.F.,Weissman K.J.
The structure of docking domains in modular polyketide synthases.
Chem. Biol.
10
723-731
2003
159049
Tang Y.,Chen A.Y.,Kim C.Y.,Cane D.E.,Khosla C.
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase.
Chem. Biol.
14
931-943
2007
159050
Keatinge-Clay A.
Crystal structure of the erythromycin polyketide synthase dehydratase.
J. Mol. Biol.
384
941-953
2008