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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)DescriptionActionsGraphical viewLength
Sitei155Important for substrate specificity of the beta-ketoacyl synthase 11 Publication1
Sitei156Important for substrate specificity of the beta-ketoacyl synthase 11 Publication1
Active sitei202Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication1
Active sitei651Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation1
Active sitei1267For C2-type beta-ketoacyl reductase 1 and probable racemase activityBy similarity1 Publication1
Active sitei1661Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1
Active sitei2105Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation1
Active sitei2409Proton acceptor, for dehydratase activity1 Publication1
Active sitei2571Proton donor; for dehydratase activity1 Publication1
Active sitei2874For enoyl reductase activity1 Publication1
Binding sitei3250NADP 2By similarity1
Active sitei3287For beta-ketoacyl reductase 2 activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi2964 – 2973NADP 11 Publication10
Nucleotide bindingi3149 – 3152NADP 2Curated4
Nucleotide bindingi3173 – 3176NADP 2Curated4
Nucleotide bindingi3202 – 3203NADP 2Curated2
Nucleotide bindingi3272 – 3273NADP 2Curated2

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)DescriptionActionsGraphical viewLength
Mutagenesisi1254S → F: Produces tetraketide lactone shunt and also 6-deoxyerythronolide (6-dEB). 1 Publication1
Mutagenesisi1267Y → F: Produces tetraketide lactone shunt and also 6-deoxyerythronolide (6-dEB). 1 Publication1
Mutagenesisi2640R → D: Decreased production of the erythromycin precursor 6-deoxyerythronolide B (6-dEB). 1 Publication1
Mutagenesisi2874Y → V: Switches the configuration of the C-2 methyl group of the product. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001802942 – 35676-deoxyerythronolide-B synthase EryA2, modules 3 and 4Add BLAST3566

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1430O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei3448O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

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

13567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 41Combined sources9
Helixi49 – 57Combined sources9
Beta strandi68 – 70Combined sources3
Helixi74 – 77Combined sources4
Beta strandi92 – 94Combined sources3
Beta strandi99 – 102Combined sources4
Helixi104 – 107Combined sources4
Helixi111 – 115Combined sources5
Helixi119 – 134Combined sources16
Helixi139 – 142Combined sources4
Beta strandi148 – 152Combined sources5
Turni158 – 161Combined sources4
Helixi171 – 174Combined sources4
Helixi178 – 189Combined sources12
Beta strandi195 – 199Combined sources5
Helixi201 – 203Combined sources3
Helixi204 – 217Combined sources14
Beta strandi222 – 230Combined sources9
Helixi236 – 242Combined sources7
Turni243 – 245Combined sources3
Beta strandi268 – 276Combined sources9
Helixi277 – 282Combined sources6
Beta strandi289 – 298Combined sources10
Helixi310 – 323Combined sources14
Helixi328 – 330Combined sources3
Beta strandi333 – 335Combined sources3
Turni342 – 344Combined sources3
Helixi345 – 354Combined sources10
Beta strandi357 – 359Combined sources3
Beta strandi366 – 369Combined sources4
Helixi372 – 375Combined sources4
Helixi379 – 381Combined sources3
Helixi382 – 396Combined sources15
Beta strandi406 – 408Combined sources3
Beta strandi415 – 421Combined sources7
Beta strandi430 – 433Combined sources4
Beta strandi436 – 442Combined sources7
Beta strandi446 – 455Combined sources10
Beta strandi472 – 480Combined sources9
Helixi481 – 494Combined sources14
Beta strandi497 – 499Combined sources3
Helixi502 – 511Combined sources10
Beta strandi517 – 526Combined sources10
Helixi527 – 539Combined sources13
Beta strandi547 – 551Combined sources5
Beta strandi559 – 563Combined sources5
Turni571 – 574Combined sources4
Helixi575 – 579Combined sources5
Helixi582 – 594Combined sources13
Helixi596 – 598Combined sources3
Helixi603 – 608Combined sources6
Helixi619 – 639Combined sources21
Beta strandi645 – 649Combined sources5
Helixi653 – 660Combined sources8
Helixi666 – 681Combined sources16
Turni682 – 685Combined sources4
Beta strandi688 – 694Combined sources7
Helixi696 – 701Combined sources6
Helixi704 – 706Combined sources3
Beta strandi714 – 717Combined sources4
Beta strandi720 – 725Combined sources6
Helixi727 – 737Combined sources11
Turni738 – 741Combined sources4
Helixi756 – 758Combined sources3
Turni759 – 761Combined sources3
Helixi762 – 769Combined sources8
Beta strandi778 – 782Combined sources5
Turni784 – 786Combined sources3
Beta strandi788 – 790Combined sources3
Helixi792 – 794Combined sources3
Helixi797 – 805Combined sources9
Helixi810 – 819Combined sources10
Beta strandi824 – 827Combined sources4
Beta strandi829 – 831Combined sources3
Helixi835 – 843Combined sources9
Beta strandi852 – 854Combined sources3
Helixi863 – 875Combined sources13
Turni876 – 878Combined sources3
Helixi883 – 886Combined sources4
Helixi2368 – 2370Combined sources3
Beta strandi2380 – 2385Combined sources6
Turni2387 – 2389Combined sources3
Beta strandi2392 – 2398Combined sources7
Turni2400 – 2402Combined sources3
Helixi2404 – 2408Combined sources5
Beta strandi2409 – 2411Combined sources3
Beta strandi2414 – 2416Combined sources3
Helixi2419 – 2433Combined sources15
Beta strandi2437 – 2443Combined sources7
Beta strandi2454 – 2463Combined sources10
Beta strandi2469 – 2477Combined sources9
Helixi2482 – 2484Combined sources3
Beta strandi2488 – 2496Combined sources9
Helixi2522 – 2528Combined sources7
Beta strandi2531 – 2533Combined sources3
Helixi2535 – 2537Combined sources3
Beta strandi2540 – 2546Combined sources7
Beta strandi2549 – 2555Combined sources7
Helixi2567 – 2575Combined sources9
Helixi2576 – 2579Combined sources4
Beta strandi2590 – 2600Combined sources11
Beta strandi2605 – 2613Combined sources9
Beta strandi2618 – 2624Combined sources7
Beta strandi2630 – 2640Combined sources11
Helixi3498 – 3511Combined sources14
Helixi3518 – 3536Combined sources19
Helixi3550 – 3562Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PZQNMR-A/B3490-3547[»]
1PZRNMR-A/B3548-3567[»]
2QO3X-ray2.59A/B27-922[»]
3EL6X-ray1.85A2362-2653[»]
ProteinModelPortaliQ03132.
SMRiQ03132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1397 – 1467Acyl carrier 1PROSITE-ProRule annotationAdd BLAST71
Domaini3415 – 3485Acyl carrier 2PROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 1467Module 3CuratedAdd BLAST1435
Regioni33 – 458Beta-ketoacyl synthase 1CuratedAdd BLAST426
Regioni560 – 880Acyltransferase 1CuratedAdd BLAST321
Regioni1132 – 1297C2-type beta-ketoacyl reductase 1CuratedAdd BLAST166
Regioni1491 – 3485Module 4CuratedAdd BLAST1995
Regioni1491 – 1915Beta-ketoacyl synthase 2CuratedAdd BLAST425
Regioni2015 – 2331Acyltransferase 2CuratedAdd BLAST317
Regioni2377 – 2645DehydrataseCuratedAdd BLAST269
Regioni2831 – 3131Enoyl reductaseCuratedAdd BLAST301
Regioni3141 – 3317Beta-ketoacyl reductase 2CuratedAdd BLAST177

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)DescriptionActionsGraphical viewLength
Sequence conflicti438R → A in CAA44448 (PubMed:1740151).Curated1
Sequence conflicti480T → S in CAA44448 (PubMed:1740151).Curated1
Sequence conflicti1241L → F in CAA44448 (PubMed:1740151).Curated1
Sequence conflicti2664G → V in CAA44448 (PubMed:1740151).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PZQNMR-A/B3490-3547[»]
1PZRNMR-A/B3548-3567[»]
2QO3X-ray2.59A/B27-922[»]
3EL6X-ray1.85A2362-2653[»]
ProteinModelPortaliQ03132.
SMRiQ03132.
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...

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: November 30, 2016
This is version 137 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.