Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

6-deoxyerythronolide-B synthase EryA1, modules 1 and 2

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).1 Publication2 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 3 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
Active sitei145 – 1451Acyl-ester intermediate; for acyltransferase 1 activityCurated
Active sitei677 – 6771Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation
Active sitei1128 – 11281Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotationBy similarity
Binding sitei1723 – 17231NADP 11 Publication
Sitei1748 – 17481Could be the principal determinant of stereospecificity1 Publication
Active sitei1760 – 17601For beta-ketoacyl reductase 1 activityBy similarity1 Publication
Active sitei2148 – 21481Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation
Active sitei2598 – 25981Acyl-ester intermediate; for acyltransferase 3 activityPROSITE-ProRule annotationBy similarity
Binding sitei3168 – 31681NADP 2Curated
Active sitei3203 – 32031For beta-ketoacyl reductase 2 activityCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1621 – 16244NADP 11 Publication
Nucleotide bindingi1644 – 16474NADP 11 Publication
Nucleotide bindingi1673 – 16742NADP 11 Publication
Nucleotide bindingi1745 – 17462NADP 11 Publication
Nucleotide bindingi3065 – 30684NADP 2Curated
Nucleotide bindingi3088 – 30914NADP 2Curated
Nucleotide bindingi3117 – 31182NADP 2Curated
Nucleotide bindingi3188 – 31892NADP 2Curated

GO - Molecular functioni

  • erythronolide synthase activity Source: UniProtKB
  • 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-17077.
BRENDAi2.3.1.94. 5518.
UniPathwayiUPA00240.

Names & Taxonomyi

Protein namesi
Recommended name:
6-deoxyerythronolide-B synthase EryA1, modules 1 and 2Curated (EC:2.3.1.941 Publication)
Short name:
DEBS 11 Publication
Alternative name(s):
6-deoxyerythronolide B synthase I1 Publication
Erythronolide synthase
ORF CCurated
Gene namesi
Name:eryA
OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifieri1836 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeSaccharopolyspora

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1705 – 17051D → A: Still able to produce the triketide lactone (TKL), albeit at reduced titer (40%) compared to the wild-type. Still able to produce the triketide lactone (TKL), albeit at reduced titer (10%) compared to the wild-type; when associated with G-1748. 1 Publication
Mutagenesisi1748 – 17481F → G: Still able to produce the triketide lactone (TKL), albeit at reduced titer (10%) compared to the wild-type; when associated with A-1705. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349134916-deoxyerythronolide-B synthase EryA1, modules 1 and 2PRO_0000180293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei1921 – 19211O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3367 – 33671O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Homodimer (PubMed:16564177). 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.2 Publications1 Publication

Protein-protein interaction databases

STRINGi405948.SeryN2_010100034325.

Structurei

Secondary structure

1
3491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1397 – 13993Combined sources
Beta strandi1400 – 14089Combined sources
Beta strandi1419 – 14257Combined sources
Helixi1431 – 144212Combined sources
Turni1443 – 14453Combined sources
Beta strandi1447 – 14526Combined sources
Helixi1459 – 14668Combined sources
Beta strandi1473 – 14775Combined sources
Turni1479 – 14824Combined sources
Helixi1490 – 14923Combined sources
Helixi1494 – 150815Combined sources
Beta strandi1515 – 15217Combined sources
Helixi1534 – 15363Combined sources
Helixi1537 – 154913Combined sources
Helixi1551 – 15533Combined sources
Beta strandi1554 – 15607Combined sources
Helixi1568 – 15769Combined sources
Beta strandi1584 – 15885Combined sources
Beta strandi1591 – 15999Combined sources
Beta strandi1613 – 16186Combined sources
Turni1619 – 16213Combined sources
Helixi1623 – 163513Combined sources
Beta strandi1638 – 16469Combined sources
Helixi1647 – 16493Combined sources
Helixi1653 – 166210Combined sources
Beta strandi1666 – 16716Combined sources
Helixi1677 – 16859Combined sources
Beta strandi1689 – 16913Combined sources
Beta strandi1693 – 16986Combined sources
Helixi1708 – 17103Combined sources
Helixi1713 – 17197Combined sources
Helixi1721 – 173414Combined sources
Beta strandi1740 – 17478Combined sources
Helixi1748 – 17514Combined sources
Turni1758 – 17603Combined sources
Helixi1761 – 177616Combined sources
Beta strandi1782 – 17865Combined sources
Beta strandi1789 – 17935Combined sources
Turni1804 – 18074Combined sources
Helixi1813 – 182513Combined sources
Helixi1838 – 18458Combined sources
Beta strandi1847 – 18493Combined sources
Turni1853 – 18564Combined sources
Helixi1858 – 18614Combined sources
Helixi3318 – 33225Combined sources
Helixi3327 – 334519Combined sources
Helixi3351 – 33533Combined sources
Beta strandi3356 – 33583Combined sources
Helixi3360 – 33634Combined sources
Helixi3368 – 337710Combined sources
Helixi3378 – 33803Combined sources
Helixi3389 – 33924Combined sources
Helixi3396 – 340712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FR0X-ray1.81A1391-1872[»]
2FR1X-ray1.79A1391-1872[»]
2JU1NMR-A3318-3408[»]
2JU2NMR-A3318-3408[»]
ProteinModelPortaliQ03131.
SMRiQ03131. Positions 1395-1862, 3318-3408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03131.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini414 – 48471Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini1888 – 195871Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Domaini3334 – 340471Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 484484Loading domainCuratedAdd
BLAST
Regioni57 – 372316Acyltransferase 1CuratedAdd
BLAST
Regioni507 – 19581452Module 1CuratedAdd
BLAST
Regioni507 – 931425Beta-ketoacyl synthase 1CuratedAdd
BLAST
Regioni1031 – 1352322Acyltransferase 2CuratedAdd
BLAST
Regioni1613 – 1790178Beta-ketoacyl reductase 1CuratedAdd
BLAST
Regioni1982 – 34041423Module 2CuratedAdd
BLAST
Regioni1982 – 2405424Beta-ketoacyl synthase 2CuratedAdd
BLAST
Regioni2508 – 2827320Acyltransferase 3CuratedAdd
BLAST
Regioni3057 – 3233177Beta-ketoacyl reductase 2CuratedAdd
BLAST

Sequence similaritiesi

Contains 3 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4107EEY. Bacteria.
COG3321. LUCA.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
3.40.366.10. 6 hits.
3.40.47.10. 4 hits.
3.40.50.720. 3 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
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.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 3 hits.
PF16197. KAsynt_C_assoc. 2 hits.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00827. PKS_AT. 3 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
SSF51735. SSF51735. 4 hits.
SSF52151. SSF52151. 6 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 3 hits.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03131-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGPRSRTTS RRTPVRIGAV VVASSTSELL DGLAAVADGR PHASVVRGVA
60 70 80 90 100
RPSAPVVFVF PGQGAQWAGM AGELLGESRV FAAAMDACAR AFEPVTDWTL
110 120 130 140 150
AQVLDSPEQS RRVEVVQPAL FAVQTSLAAL WRSFGVTPDA VVGHSIGELA
160 170 180 190 200
AAHVCGAAGA ADAARAAALW SREMIPLVGN GDMAAVALSA DEIEPRIARW
210 220 230 240 250
DDDVVLAGVN GPRSVLLTGS PEPVARRVQE LSAEGVRAQV INVSMAAHSA
260 270 280 290 300
QVDDIAEGMR SALAWFAPGG SEVPFYASLT GGAVDTRELV ADYWRRSFRL
310 320 330 340 350
PVRFDEAIRS ALEVGPGTFV EASPHPVLAA ALQQTLDAEG SSAAVVPTLQ
360 370 380 390 400
RGQGGMRRFL LAAAQAFTGG VAVDWTAAYD DVGPNPALCR SSRRPRRKTS
410 420 430 440 450
RPSPASTGTR HRTCCERLLA VVNGETAALA GREADAEATF RELGLDSVLA
460 470 480 490 500
AQLRAKVSAA IGREVNIALL YDHPTPRALA EALAAGTEVA QRETRARTNE
510 520 530 540 550
AAPGEPVAVV AMACRLPGGV STPEEFWELL SEGRDAVAGL PTDRGWDLDS
560 570 580 590 600
LFHPDPTRSG TAHQRGGGFL TEATAFDPAF FGMSPREALA VDPQQRLMLE
610 620 630 640 650
LSWEVLERAG IPPTSLQASP TGVFVGLIPQ EYGPRLAEGG EGVEGYLMTG
660 670 680 690 700
TTTSVASGRI AYTLGLEGPA ISVDTACSSS LVAVHLACQS LRRGESSLAM
710 720 730 740 750
AGGVTVMPTP GMLVDFSRMN SLAPDGRCKA FSAGANGFGM AEGAGMLLLE
760 770 780 790 800
RLSDARRNGH PVLAVLRGTA VNSDGASNGL SAPNGRAQVR VIQQALAESG
810 820 830 840 850
LGPADIDAVE AHGTGTRLGD PIEARALFEA YGRDREQPLH LGSVKSNLGH
860 870 880 890 900
TQAAAGVAGV IKMVLAMRAG TLPRTLHASE RSKEIDWSSG AISLLDEPEP
910 920 930 940 950
WPAGARPRRA GVSSFGISGT NAHAIIEEAP QVVEGERVEA GDVVAPWVLS
960 970 980 990 1000
ASSAEGLRAQ AARLAAHLRE HPGQDPRDIA YSLATGRAAL PHRAAFAPVD
1010 1020 1030 1040 1050
ESAALRVLDG LATGNADGAA VGTSRAQQRA VFVFPGQGWQ WAGMAVDLLD
1060 1070 1080 1090 1100
TSPVFAAALR ECADALEPHL DFEVIPFLRA EAARREQDAA LSTERVDVVQ
1110 1120 1130 1140 1150
PVMFAVMVSL ASMWRAHGVE PAAVIGHSQG EIAAACVAGA LSLDDAARVV
1160 1170 1180 1190 1200
ALRSRVIATM PGNKGMASIA APAGEVRARI GDRVEIAAVN GPRSVVVAGD
1210 1220 1230 1240 1250
SDELDRLVAS CTTECIRAKR LAVDYASHSS HVETIRDALH AELGEDFHPL
1260 1270 1280 1290 1300
PGFVPFFSTV TGRWTQPDEL DAGYWYRNLR RTVRFADAVR ALAEQGYRTF
1310 1320 1330 1340 1350
LEVSAHPILT AAIEEIGDGS GADLSAIHSL RRGDGSLADF GEALSRAFAA
1360 1370 1380 1390 1400
GVAVDWESVH LGTGARRVPL PTYPFQRERV WLEPKPVARR STEVDEVSAL
1410 1420 1430 1440 1450
RYRIEWRPTG AGEPARLDGT WLVAKYAGTA DETSTAAREA LESAGARVRE
1460 1470 1480 1490 1500
LVVDARCGRD ELAERLRSVG EVAGVLSLLA VDEAEPEEAP LALASLADTL
1510 1520 1530 1540 1550
SLVQAMVSAE LGCPLWTVTE SAVATGPFER VRNAAHGALW GVGRVIALEN
1560 1570 1580 1590 1600
PAVWGGLVDV PAGSVAELAR HLAAVVSGGA GEDQLALRAD GVYGRRWVRA
1610 1620 1630 1640 1650
AAPATDDEWK PTGTVLVTGG TGGVGGQIAR WLARRGAPHL LLVSRSGPDA
1660 1670 1680 1690 1700
DGAGELVAEL EALGARTTVA ACDVTDRESV RELLGGIGDD VPLSAVFHAA
1710 1720 1730 1740 1750
ATLDDGTVDT LTGERIERAS RAKVLGARNL HELTRELDLT AFVLFSSFAS
1760 1770 1780 1790 1800
AFGAPGLGGY APGNAYLDGL AQQRRSDGLP ATAVAWGTWA GSGMAEGAVA
1810 1820 1830 1840 1850
DRFRRHGVIE MPPETACRAL QNALDRAEVC PIVIDVRWDR FLLAYTAQRP
1860 1870 1880 1890 1900
TRLFDEIDDA RRAAPQAPAE PRVGALASLP APEREEALFE LVRSHAAAVL
1910 1920 1930 1940 1950
GHASAERVPA DQAFAELGVD SLSALELRNR LGAATGVRLP TTTVFDHPDV
1960 1970 1980 1990 2000
RTLAAHLAAE LGGATGAEQA APATTAPVDE PIAIVGMACR LPGEVDSPER
2010 2020 2030 2040 2050
LWELITSGRD SAAEVPDDRG WVPDELMASD AAGTRAHGNF MAGAGDFDAA
2060 2070 2080 2090 2100
FFGISPREAL AMDPQQRQAL ETTWEALESA GIPPETLRGS DTGVFVGMSH
2110 2120 2130 2140 2150
QGYATGRPRP EDGVDGYLLT GNTASVASGR IAYVLGLEGP ALTVDTACSS
2160 2170 2180 2190 2200
SLVALHTACG SLRDGDCGLA VAGGVSVMAG PEVFTEFSRQ GALSPDGRCK
2210 2220 2230 2240 2250
PFSDEADGFG LGEGSAFVVL QRLSDARREG RRVLGVVAGS AVNQDGASNG
2260 2270 2280 2290 2300
LSAPSGVAQQ RVIRRAWARA GITGADVAVV EAHGTGTRLG DPVEASALLA
2310 2320 2330 2340 2350
TYGKSRGSSG PVLLGSVKSN IGHAQAAAGV AGVIKVLLGL ERGVVPPMLC
2360 2370 2380 2390 2400
RGERSGLIDW SSGEIELADG VREWSPAADG VRRAGVSAFG VSGTNAHVII
2410 2420 2430 2440 2450
AEPPEPEPVP QPRRMLPATG VVPVVLSART GAALRAQAGR LADHLAAHPG
2460 2470 2480 2490 2500
IAPADVSWTM ARARQHFEER AAVLAADTAE AVHRLRAVAD GAVVPGVVTG
2510 2520 2530 2540 2550
SASDGGSVFV FPGQGAQWEG MARELLPVPV FAESIAECDA VLSEVAGFSV
2560 2570 2580 2590 2600
SEVLEPRPDA PSLERVDVVQ PVLFAVMVSL ARLWRACGAV PSAVIGHSQG
2610 2620 2630 2640 2650
EIAAAVVAGA LSLEDGMRVV ARRSRAVRAV AGRGSMLSVR GGRSDVEKLL
2660 2670 2680 2690 2700
ADDSWTGRLE VAAVNGPDAV VVAGDAQAAR EFLEYCEGVG IRARAIPVDY
2710 2720 2730 2740 2750
ASHTAHVEPV RDELVQALAG ITPRRAEVPF FSTLTGDFLD GTELDAGYWY
2760 2770 2780 2790 2800
RNLRHPVEFH SAVQALTDQG YATFIEVSPH PVLASSVQET LDDAESDAAV
2810 2820 2830 2840 2850
LGTLERDAGD ADRFLTALAD AHTRGVAVDW EAVLGRAGLV DLPGYPFQGK
2860 2870 2880 2890 2900
RFWLLPDRTT PRDELDGWFY RVDWTEVPRS EPAALRGRWL VVVPEGHEED
2910 2920 2930 2940 2950
GWTVEVRSAL AEAGAEPEVT RGVGGLVGDC AGVVSLLALE GDGAVQTLVL
2960 2970 2980 2990 3000
VRELDAEGID APLWTVTFGA VDAGSPVARP DQAKLWGLGQ VASLERGPRW
3010 3020 3030 3040 3050
TGLVDLPHMP DPELRGRLTA VLAGSEDQVA VRADAVRARR LSPAHVTATS
3060 3070 3080 3090 3100
EYAVPGGTIL VTGGTAGLGA EVARWLAGRG AEHLALVSRR GPDTEGVGDL
3110 3120 3130 3140 3150
TAELTRLGAR VSVHACDVSS REPVRELVHG LIEQGDVVRG VVHAAGLPQQ
3160 3170 3180 3190 3200
VAINDMDEAA FDEVVAAKAG GAVHLDELCS DAELFLLFSS GAGVWGSARQ
3210 3220 3230 3240 3250
GAYAAGNAFL DAFARHRRGR GLPATSVAWG LWAAGGMTGD EEAVSFLRER
3260 3270 3280 3290 3300
GVRAMPVPRA LAALDRVLAS GETAVVVTDV DWPAFAESYT AARPRPLLDR
3310 3320 3330 3340 3350
IVTTAPSERA GEPETESLRD RLAGLPRAER TAELVRLVRT STATVLGHDD
3360 3370 3380 3390 3400
PKAVRATTPF KELGFDSLAA VRLRNLLNAA TGLRLPSTLV FDHPNASAVA
3410 3420 3430 3440 3450
GFLDAELGTE VRGEAPSALA GLDALEGALP EVPATEREEL VQRLERMLAA
3460 3470 3480 3490
LRPVAQAADA SGTGANPSGD DLGEAGVDEL LEALGRELDG D
Length:3,491
Mass (Da):365,029
Last modified:October 1, 1993 - v1
Checksum:i682BFC32C90FA8C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63676 Genomic DNA. Translation: AAA26493.2.
L07626 Genomic DNA. Translation: AAA26504.1.
PIRiT43231.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63676 Genomic DNA. Translation: AAA26493.2.
L07626 Genomic DNA. Translation: AAA26504.1.
PIRiT43231.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FR0X-ray1.81A1391-1872[»]
2FR1X-ray1.79A1391-1872[»]
2JU1NMR-A3318-3408[»]
2JU2NMR-A3318-3408[»]
ProteinModelPortaliQ03131.
SMRiQ03131. Positions 1395-1862, 3318-3408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi405948.SeryN2_010100034325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107EEY. Bacteria.
COG3321. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00240.
BioCyciMetaCyc:MONOMER-17077.
BRENDAi2.3.1.94. 5518.

Miscellaneous databases

EvolutionaryTraceiQ03131.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
3.40.366.10. 6 hits.
3.40.47.10. 4 hits.
3.40.50.720. 3 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
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.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 3 hits.
PF16197. KAsynt_C_assoc. 2 hits.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00827. PKS_AT. 3 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
SSF51735. SSF51735. 4 hits.
SSF52151. SSF52151. 6 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 3 hits.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERYA1_SACER
AccessioniPrimary (citable) accession number: Q03131
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 114 of the entry and version 1 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. KR controls the stereochemistry of the beta-hydroxyl group of a polyketide (PubMed:16564177).1 Publication1 Publication

Keywords - Technical termi

3D-structure, 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.