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Protein

6-deoxyerythronolide-B synthase EryA2, modules 3 and 4

Gene

eryA

Organism
Saccharopolyspora erythraea (Streptomyces erythraeus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of antibiotic erythromycin via the biosynthesis of its aglycone precursor, 6-deoxyerythronolide B (6-dEB).2 Publications4 Publications

Catalytic activityi

Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+.1 Publication

Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 2 phosphopantetheines covalently.Curated

Pathwayi: erythromycin biosynthesis

This protein is involved in the pathway erythromycin biosynthesis, which is part of Antibiotic biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway erythromycin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1551Important for substrate specificity of the beta-ketoacyl synthase 11 Publication
Sitei156 – 1561Important for substrate specificity of the beta-ketoacyl synthase 11 Publication
Active sitei202 – 2021Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication
Active sitei651 – 6511Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation
Active sitei1267 – 12671C2-type beta-ketoacyl reductase 1 (with a probable racemase activity)By similarity1 Publication
Active sitei1661 – 16611Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation
Active sitei2105 – 21051Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation
Active sitei2409 – 24091Proton acceptor, for dehydratase activity1 Publication
Active sitei2571 – 25711Proton donor; for dehydratase activity1 Publication
Active sitei2874 – 28741For enoyl reductase activity1 Publication
Binding sitei3250 – 32501NADP 2By similarity
Active sitei3287 – 32871For beta-ketoacyl reductase 2 activityCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2964 – 297310NADP 11 Publication
Nucleotide bindingi3149 – 31524NADP 2Curated
Nucleotide bindingi3173 – 31764NADP 2Curated
Nucleotide bindingi3202 – 32032NADP 2Curated
Nucleotide bindingi3272 – 32732NADP 2Curated

GO - Molecular functioni

  • cofactor binding Source: InterPro
  • erythronolide synthase activity Source: UniProtKB
  • oxidoreductase activity Source: InterPro
  • phosphopantetheine binding Source: UniProtKB

GO - Biological processi

  • macrolide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17078.
BRENDAi2.3.1.94. 5518.
UniPathwayiUPA00240.

Names & Taxonomyi

Protein namesi
Recommended name:
6-deoxyerythronolide-B synthase EryA2, modules 3 and 4Curated (EC:2.3.1.941 Publication)
Short name:
DEBS 21 Publication
Alternative name(s):
6-deoxyerythronolide B synthase II1 Publication
Erythronolide synthase
ORF B1 Publication
Gene namesi
Name:eryA1 Publication
OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifieri1836 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeSaccharopolyspora

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to produce 6-deoxyerythronolide (6-dEB), however a tetraketide lactone shunt is produced.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1254 – 12541S → F: Produces tetraketide lactone shunt and also 6-deoxyerythronolide (6-dEB). 1 Publication
Mutagenesisi1267 – 12671Y → F: Produces tetraketide lactone shunt and also 6-deoxyerythronolide (6-dEB). 1 Publication
Mutagenesisi2640 – 26401R → D: Decreased production of the erythromycin precursor 6-deoxyerythronolide B (6-dEB). 1 Publication
Mutagenesisi2874 – 28741Y → V: Switches the configuration of the C-2 methyl group of the product. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 356735666-deoxyerythronolide-B synthase EryA2, modules 3 and 4PRO_0000180294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1430 – 14301O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3448 – 34481O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Homodimer (PubMed:12954331, PubMed:17719492, PubMed:18952099). Erythronolide synthase is composed of EryAI, EryAII and EryAIII multimodular (2 modules) polypeptides each coding for a functional synthase subunit which participates in 2 of the six FAS-like elongation steps required for formation of the polyketide. Module 1, 2, 3, 4, 5, and 6 participating in biosynthesis steps 1, 2, 3, 4, 5, and 6, respectively.3 Publications3 Publications

Structurei

Secondary structure

1
3567
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 419Combined sources
Helixi49 – 579Combined sources
Beta strandi68 – 703Combined sources
Helixi74 – 774Combined sources
Beta strandi92 – 943Combined sources
Beta strandi99 – 1024Combined sources
Helixi104 – 1074Combined sources
Helixi111 – 1155Combined sources
Helixi119 – 13416Combined sources
Helixi139 – 1424Combined sources
Beta strandi148 – 1525Combined sources
Turni158 – 1614Combined sources
Helixi171 – 1744Combined sources
Helixi178 – 18912Combined sources
Beta strandi195 – 1995Combined sources
Helixi201 – 2033Combined sources
Helixi204 – 21714Combined sources
Beta strandi222 – 2309Combined sources
Helixi236 – 2427Combined sources
Turni243 – 2453Combined sources
Beta strandi268 – 2769Combined sources
Helixi277 – 2826Combined sources
Beta strandi289 – 29810Combined sources
Helixi310 – 32314Combined sources
Helixi328 – 3303Combined sources
Beta strandi333 – 3353Combined sources
Turni342 – 3443Combined sources
Helixi345 – 35410Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi366 – 3694Combined sources
Helixi372 – 3754Combined sources
Helixi379 – 3813Combined sources
Helixi382 – 39615Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi415 – 4217Combined sources
Beta strandi430 – 4334Combined sources
Beta strandi436 – 4427Combined sources
Beta strandi446 – 45510Combined sources
Beta strandi472 – 4809Combined sources
Helixi481 – 49414Combined sources
Beta strandi497 – 4993Combined sources
Helixi502 – 51110Combined sources
Beta strandi517 – 52610Combined sources
Helixi527 – 53913Combined sources
Beta strandi547 – 5515Combined sources
Beta strandi559 – 5635Combined sources
Turni571 – 5744Combined sources
Helixi575 – 5795Combined sources
Helixi582 – 59413Combined sources
Helixi596 – 5983Combined sources
Helixi603 – 6086Combined sources
Helixi619 – 63921Combined sources
Beta strandi645 – 6495Combined sources
Helixi653 – 6608Combined sources
Helixi666 – 68116Combined sources
Turni682 – 6854Combined sources
Beta strandi688 – 6947Combined sources
Helixi696 – 7016Combined sources
Helixi704 – 7063Combined sources
Beta strandi714 – 7174Combined sources
Beta strandi720 – 7256Combined sources
Helixi727 – 73711Combined sources
Turni738 – 7414Combined sources
Helixi756 – 7583Combined sources
Turni759 – 7613Combined sources
Helixi762 – 7698Combined sources
Beta strandi778 – 7825Combined sources
Turni784 – 7863Combined sources
Beta strandi788 – 7903Combined sources
Helixi792 – 7943Combined sources
Helixi797 – 8059Combined sources
Helixi810 – 81910Combined sources
Beta strandi824 – 8274Combined sources
Beta strandi829 – 8313Combined sources
Helixi835 – 8439Combined sources
Beta strandi852 – 8543Combined sources
Helixi863 – 87513Combined sources
Turni876 – 8783Combined sources
Helixi883 – 8864Combined sources
Helixi2368 – 23703Combined sources
Beta strandi2380 – 23856Combined sources
Turni2387 – 23893Combined sources
Beta strandi2392 – 23987Combined sources
Turni2400 – 24023Combined sources
Helixi2404 – 24085Combined sources
Beta strandi2409 – 24113Combined sources
Beta strandi2414 – 24163Combined sources
Helixi2419 – 243315Combined sources
Beta strandi2437 – 24437Combined sources
Beta strandi2454 – 246310Combined sources
Beta strandi2469 – 24779Combined sources
Helixi2482 – 24843Combined sources
Beta strandi2488 – 24969Combined sources
Helixi2522 – 25287Combined sources
Beta strandi2531 – 25333Combined sources
Helixi2535 – 25373Combined sources
Beta strandi2540 – 25467Combined sources
Beta strandi2549 – 25557Combined sources
Helixi2567 – 25759Combined sources
Helixi2576 – 25794Combined sources
Beta strandi2590 – 260011Combined sources
Beta strandi2605 – 26139Combined sources
Beta strandi2618 – 26247Combined sources
Beta strandi2630 – 264011Combined sources
Helixi3498 – 351114Combined sources
Helixi3518 – 353619Combined sources
Helixi3550 – 356213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PZQNMR-A/B3490-3547[»]
1PZRNMR-A/B3548-3567[»]
2QO3X-ray2.59A/B27-922[»]
3EL6X-ray1.85A2362-2653[»]
ProteinModelPortaliQ03132.
SMRiQ03132. Positions 29-908, 1487-2359, 3397-3488, 3490-3547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1397 – 146771Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini3415 – 348571Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 14671435Module 3CuratedAdd
BLAST
Regioni33 – 458426Beta-ketoacyl synthase 1CuratedAdd
BLAST
Regioni560 – 880321Acyltransferase 1CuratedAdd
BLAST
Regioni1132 – 1297166C2-type beta-ketoacyl reductase 1CuratedAdd
BLAST
Regioni1491 – 34851995Module 4CuratedAdd
BLAST
Regioni1491 – 1915425Beta-ketoacyl synthase 2CuratedAdd
BLAST
Regioni2015 – 2331317Acyltransferase 2CuratedAdd
BLAST
Regioni2377 – 2645269DehydrataseCuratedAdd
BLAST
Regioni2831 – 3131301Enoyl reductaseCuratedAdd
BLAST
Regioni3141 – 3317177Beta-ketoacyl reductase 2CuratedAdd
BLAST

Sequence similaritiesi

Contains 2 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.720. 3 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR015357. Erythronolide_synth_docking.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR015083. Polyketide_synth_docking.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF08990. Docking. 1 hit.
PF09277. Erythro-docking. 1 hit.
PF16197. KAsynt_C_assoc. 2 hits.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 2 hits.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
[Graphical view]
SUPFAMiSSF101166. SSF101166. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 5 hits.
SSF52151. SSF52151. 4 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDSEKVAEY LRRATLDLRA ARQRIRELES DPIAIVSMAC RLPGGVNTPQ
60 70 80 90 100
RLWELLREGG ETLSGFPTDR GWDLARLHHP DPDNPGTSYV DKGGFLDDAA
110 120 130 140 150
GFDAEFFGVS PREAAAMDPQ QRLLLETSWE LVENAGIDPH SLRGTATGVF
160 170 180 190 200
LGVAKFGYGE DTAAAEDVEG YSVTGVAPAV ASGRISYTMG LEGPSISVDT
210 220 230 240 250
ACSSSLVALH LAVESLRKGE SSMAVVGGAA VMATPGVFVD FSRQRALAAD
260 270 280 290 300
GRSKAFGAGA DGFGFSEGVT LVLLERLSEA RRNGHEVLAV VRGSALNQDG
310 320 330 340 350
ASNGLSAPSG PAQRRVIRQA LESCGLEPGD VDAVEAHGTG TALGDPIEAN
360 370 380 390 400
ALLDTYGRDR DADRPLWLGS VKSNIGHTQA AAGVTGLLKV VLALRNGELP
410 420 430 440 450
ATLHVEEPTP HVDWSSGGVA LLAGNQPWRR GERTRRARVS AFGISGTNAH
460 470 480 490 500
VIVEEAPERE HRETTAHDGR PVPLVVSART TAALRAQAAQ IAELLERPDA
510 520 530 540 550
DLAGVGLGLA TTRARHEHRA AVVASTREEA VRGLREIAAG AATADAVVEG
560 570 580 590 600
VTEVDGRNVV FLFPGQGSQW AGMGAELLSS SPVFAGKIRA CDESMAPMQD
610 620 630 640 650
WKVSDVLRQA PGAPGLDRVD VVQPVLFAVM VSLAELWRSY GVEPAAVVGH
660 670 680 690 700
SQGEIAAAHV AGALTLEDAA KLVVGRSRLM RSLSGEGGMA AVALGEAAVR
710 720 730 740 750
ERLRPWQDRL SVAAVNGPRS VVVSGEPGAL RAFSEDCAAE GIRVRDIDVD
760 770 780 790 800
YASHSPQIER VREELLETTG DIAPRPARVT FHSTVESRSM DGTELDARYW
810 820 830 840 850
YRNLRETVRF ADAVTRLAES GYDAFIEVSP HPVVVQAVEE AVEEADGAED
860 870 880 890 900
AVVVGSLHRD GGDLSAFLRS MATAHVSGVD IRWDVALPGA APFALPTYPF
910 920 930 940 950
QRKRYWLQPA APAAASDELA YRVSWTPIEK PESGNLDGDW LVVTPLISPE
960 970 980 990 1000
WTEMLCEAIN ANGGRALRCE VDTSASRTEM AQAVAQAGTG FRGVLSLLSS
1010 1020 1030 1040 1050
DESACRPGVP AGAVGLLTLV QALGDAGVDA PVWCLTQGAV RTPADDDLAR
1060 1070 1080 1090 1100
PAQTTAHGFA QVAGLELPGR WGGVVDLPES VDDAALRLLV AVLRGGGRAE
1110 1120 1130 1140 1150
DHLAVRDGRL HGRRVVRASL PQSGSRSWTP HGTVLVTGAA SPVGDQLVRW
1160 1170 1180 1190 1200
LADRGAERLV LAGACPGDDL LAAVEEAGAS AVVCAQDAAA LREALGDEPV
1210 1220 1230 1240 1250
TALVHAGTLT NFGSISEVAP EEFAETIAAK TALLAVLDEV LGDRAVEREV
1260 1270 1280 1290 1300
YCSSVAGIWG GAGMAAYAAG SAYLDALAEH HRARGRSCTS VAWTPWALPG
1310 1320 1330 1340 1350
GAVDDGYLRE RGLRSLSADR AMRTWERVLA AGPVSVAVAD VDWPVLSEGF
1360 1370 1380 1390 1400
AATRPTALFA ELAGRGGQAE AEPDSGPTGE PAQRLAGLSP DEQQENLLEL
1410 1420 1430 1440 1450
VANAVAEVLG HESAAEINVR RAFSELGLDS LNAMALRKRL SASTGLRLPA
1460 1470 1480 1490 1500
SLVFDHPTVT ALAQHLRARL VGDADQAAVR VVGAADESEP IAIVGIGCRF
1510 1520 1530 1540 1550
PGGIGSPEQL WRVLAEGANL TTGFPADRGW DIGRLYHPDP DNPGTSYVDK
1560 1570 1580 1590 1600
GGFLTDAADF DPGFFGITPR EALAMDPQQR LMLETAWEAV ERAGIDPDAL
1610 1620 1630 1640 1650
RGTDTGVFVG MNGQSYMQLL AGEAERVDGY QGLGNSASVL SGRIAYTFGW
1660 1670 1680 1690 1700
EGPALTVDTA CSSSLVGIHL AMQALRRGEC SLALAGGVTV MSDPYTFVDF
1710 1720 1730 1740 1750
STQRGLASDG RCKAFSARAD GFALSEGVAA LVLEPLSRAR ANGHQVLAVL
1760 1770 1780 1790 1800
RGSAVNQDGA SNGLAAPNGP SQERVIRQAL AASGVPAADV DVVEAHGTGT
1810 1820 1830 1840 1850
ELGDPIEAGA LIATYGQDRD RPLRLGSVKT NIGHTQAAAG AAGVIKVVLA
1860 1870 1880 1890 1900
MRHGMLPRSL HADELSPHID WESGAVEVLR EEVPWPAGER PRRAGVSSFG
1910 1920 1930 1940 1950
VSGTNAHVIV EEAPAEQEAA RTERGPLPFV LSGRSEAVVA AQARALAEHL
1960 1970 1980 1990 2000
RDTPELGLTD AAWTLATGRA RFDVRAAVLG DDRAGVCAEL DALAEGRPSA
2010 2020 2030 2040 2050
DAVAPVTSAP RKPVLVFPGQ GAQWVGMARD LLESSEVFAE SMSRCAEALS
2060 2070 2080 2090 2100
PHTDWKLLDV VRGDGGPDPH ERVDVLQPVL FSIMVSLAEL WRAHGVTPAA
2110 2120 2130 2140 2150
VVGHSQGEIA AAHVAGALSL EAAAKVVALR SQVLRELDDQ GGMVSVGASR
2160 2170 2180 2190 2200
DELETVLARW DGRVAVAAVN GPGTSVVAGP TAELDEFFAE AEAREMKPRR
2210 2220 2230 2240 2250
IAVRYASHSP EVARIEDRLA AELGTITAVR GSVPLHSTVT GEVIDTSAMD
2260 2270 2280 2290 2300
ASYWYRNLRR PVLFEQAVRG LVEQGFDTFV EVSPHPVLLM AVEETAEHAG
2310 2320 2330 2340 2350
AEVTCVPTLR REQSGPHEFL RNLLRAHVHG VGADLRPAVA GGRPAELPTY
2360 2370 2380 2390 2400
PFEHQRFWPR PHRPADVSAL GVRGAEHPLL LAAVDVPGHG GAVFTGRLST
2410 2420 2430 2440 2450
DEQPWLAEHV VGGRTLVPGS VLVDLALAAG EDVGLPVLEE LVLQRPLVLA
2460 2470 2480 2490 2500
GAGALLRMSV GAPDESGRRT IDVHAAEDVA DLADAQWSQH ATGTLAQGVA
2510 2520 2530 2540 2550
AGPRDTEQWP PEDAVRIPLD DHYDGLAEQG YEYGPSFQAL RAAWRKDDSV
2560 2570 2580 2590 2600
YAEVSIAADE EGYAFHPVLL DAVAQTLSLG ALGEPGGGKL PFAWNTVTLH
2610 2620 2630 2640 2650
ASGATSVRVV ATPAGADAMA LRVTDPAGHL VATVDSLVVR STGEKWEQPE
2660 2670 2680 2690 2700
PRGGEGELHA LDWGRLAEPG STGRVVAADA SDLDAVLRSG EPEPDAVLVR
2710 2720 2730 2740 2750
YEPEGDDPRA AARHGVLWAA ALVRRWLEQE ELPGATLVIA TSGAVTVSDD
2760 2770 2780 2790 2800
DSVPEPGAAA MWGVIRCAQA ESPDRFVLLD TDAEPGMLPA VPDNPQLALR
2810 2820 2830 2840 2850
GDDVFVPRLS PLAPSALTLP AGTQRLVPGD GAIDSVAFEP APDVEQPLRA
2860 2870 2880 2890 2900
GEVRVDVRAT GVNFRDVLLA LGMYPQKADM GTEAAGVVTA VGPDVDAFAP
2910 2920 2930 2940 2950
GDRVLGLFQG AFAPIAVTDH RLLARVPDGW SDADAAAVPI AYTTAHYALH
2960 2970 2980 2990 3000
DLAGLRAGQS VLIHAAAGGV GMAAVALARR AGAEVLATAG PAKHGTLRAL
3010 3020 3030 3040 3050
GLDDEHIASS RETGFARKFR ERTGGRGVDV VLNSLTGELL DESADLLAED
3060 3070 3080 3090 3100
GVFVEMGKTD LRDAGDFRGR YAPFDLGEAG DDRLGEILRE VVGLLGAGEL
3110 3120 3130 3140 3150
DRLPVSAWEL GSAPAALQHM SRGRHVGKLV LTQPAPVDPD GTVLITGGTG
3160 3170 3180 3190 3200
TLGRLLARHL VTEHGVRHLL LVSRRGADAP GSDELRAEIE DLGASAEIAA
3210 3220 3230 3240 3250
CDTADRDALS ALLDGLPRPL TGVVHAAGVL ADGLVTSIDE PAVEQVLRAK
3260 3270 3280 3290 3300
VDAAWNLHEL TANTGLSFFV LFSSAASVLA GPGQGVYAAA NESLNALAAL
3310 3320 3330 3340 3350
RRTRGLPAKA LGWGLWAQAS EMTSGLGDRI ARTGVAALPT ERALALFDSA
3360 3370 3380 3390 3400
LRRGGEVVFP LSINRSALRR AEFVPEVLRG MVRAKLRAAG QAEAAGPNVV
3410 3420 3430 3440 3450
DRLAGRSESD QVAGLAELVR SHAAAVSGYG SADQLPERKA FKDLGFDSLA
3460 3470 3480 3490 3500
AVELRNRLGT ATGVRLPSTL VFDHPTPLAV AEHLRDRLFA ASPAVDIGDR
3510 3520 3530 3540 3550
LDELEKALEA LSAEDGHDDV GQRLESLLRR WNSRRADAPS TSAISEDASD
3560
DELFSMLDQR FGGGEDL
Length:3,567
Mass (Da):374,421
Last modified:January 23, 2007 - v3
Checksum:iEE6284F4738AA0C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti438 – 4381R → A in CAA44448 (PubMed:1740151).Curated
Sequence conflicti480 – 4801T → S in CAA44448 (PubMed:1740151).Curated
Sequence conflicti1241 – 12411L → F in CAA44448 (PubMed:1740151).Curated
Sequence conflicti2664 – 26641G → V in CAA44448 (PubMed:1740151).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63677 Genomic DNA. Translation: AAA26494.1.
X62569 Genomic DNA. Translation: CAA44448.1.
PIRiS23070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63677 Genomic DNA. Translation: AAA26494.1.
X62569 Genomic DNA. Translation: CAA44448.1.
PIRiS23070.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PZQNMR-A/B3490-3547[»]
1PZRNMR-A/B3548-3567[»]
2QO3X-ray2.59A/B27-922[»]
3EL6X-ray1.85A2362-2653[»]
ProteinModelPortaliQ03132.
SMRiQ03132. Positions 29-908, 1487-2359, 3397-3488, 3490-3547.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00240.
BioCyciMetaCyc:MONOMER-17078.
BRENDAi2.3.1.94. 5518.

Miscellaneous databases

EvolutionaryTraceiQ03132.

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.720. 3 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR015357. Erythronolide_synth_docking.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR015083. Polyketide_synth_docking.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF08990. Docking. 1 hit.
PF09277. Erythro-docking. 1 hit.
PF16197. KAsynt_C_assoc. 2 hits.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 2 hits.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
[Graphical view]
SUPFAMiSSF101166. SSF101166. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 5 hits.
SSF52151. SSF52151. 4 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Modular organization of genes required for complex polyketide biosynthesis."
    Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L.
    Science 252:675-679(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
  2. "6-deoxyerythronolide-B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme."
    Bevitt D.J., Cortes J., Haydock S.F., Leadlay P.F.
    Eur. J. Biochem. 204:39-49(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
    Strain: ATCC 11635 / DSM 40517 / IFO 13426 / JCM 4026 / NCIB 8594.
  3. "Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea."
    Caffrey P., Bevitt D.J., Staunton J., Leadlay P.F.
    FEBS Lett. 304:225-228(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: CA340.
  4. "Structure and mechanism of the 6-deoxyerythronolide B synthase."
    Khosla C., Tang Y., Chen A.Y., Schnarr N.A., Cane D.E.
    Annu. Rev. Biochem. 76:195-221(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, SUBUNIT.
  5. "Prediction and manipulation of the stereochemistry of enoylreduction in modular polyketide synthases."
    Kwan D.H., Sun Y., Schulz F., Hong H., Popovic B., Sim-Stark J.C., Haydock S.F., Leadlay P.F.
    Chem. Biol. 15:1231-1240(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-2874, ACTIVE SITE.
  6. "Complete biosynthesis of erythromycin A and designed analogs using E. coli as a heterologous host."
    Zhang H., Wang Y., Wu J., Skalina K., Pfeifer B.A.
    Chem. Biol. 17:1232-1240(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  7. "Structural and functional analysis of C2-type ketoreductases from modular polyketide synthases."
    Zheng J., Keatinge-Clay A.T.
    J. Mol. Biol. 410:105-117(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-1254 AND TYR-1267, DISRUPTION PHENOTYPE, REACTION MECHANISM, ACTIVE SITE.
  8. "The structure of docking domains in modular polyketide synthases."
    Broadhurst R.W., Nietlispach D., Wheatcroft M.P., Leadlay P.F., Weissman K.J.
    Chem. Biol. 10:723-731(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 3488-3547, SUBUNIT.
  9. "Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase."
    Tang Y., Chen A.Y., Kim C.Y., Cane D.E., Khosla C.
    Chem. Biol. 14:931-943(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 27-922 IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, SUBSTRATE SPECIFICITY, ACTIVE SITE, COFACTOR, SUBUNIT.
  10. "Crystal structure of the erythromycin polyketide synthase dehydratase."
    Keatinge-Clay A.
    J. Mol. Biol. 384:941-953(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2362-2653, FUNCTION, MUTAGENESIS OF ARG-2640, SUBUNIT, ACTIVE SITE.

Entry informationi

Entry nameiERYA2_SACER
AccessioniPrimary (citable) accession number: Q03132
Secondary accession number(s): Q54096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Type I modular polyketide synthases (PKSs) catalyze the step-wise condensation of simple carboxylic acid derivatives. Organizationally, type I PKSs are arranged into modules, wherein each module is comprised of a set of catalytic activities that is responsible for a single elongation of the polyketide chain and the appropriate reductive processing of the beta-keto functionality. A minimal elongation module contains an acyl transferase (AT) domain, an acyl-carrier protein (ACP) domain, and a ketosynthase (KS) domain. The AT domain is responsible for loading the methylmalonyl-CoA extender unit onto the phosphopantetheinylated ACP domain. Subsequently, the KS domain decarboxylates and then condenses the ACP-bound extender unit with the growing polyketide chain obtained from the preceding module to yield an ACP-bound beta-ketoacyl intermediate. In addition to the three core domains, each elongation module may contain up to three additional domains: a ketoreductase (KR), dehydratase (DH), and an enoyl reductase (ER) that are responsible for the reductive processing of the beta-keto functionality prior to the next extension step. The presence of a KR domain alone gives rise to a beta-hydroxyl functionality, the presence of both a KR and a DH domain generates an alkene, while the combination of KR, DH, and ER results in complete reduction to the alkane. Finally, a thioesterase (TE) domain, typically found at the terminus of the last elongation module, catalyzes the termination of polyketide biosynthesis. The activity of this domain results in cleavage of the acyl chain from the adjacent ACP and formation of the macrocyclic ring.2 Publications
C2-type beta-ketoacyl reductase 1 is unable to bind NADP and seems to act as a racemase.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.