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Protein

6-deoxyerythronolide-B synthase EryA3, modules 5 and 6

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 Publication1 Publication

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

Enzyme regulationi

Inhibited by diphenyl phosphonates derivatives such as diphenyl allylphosphonate.1 Publication

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 sitei199 – 1991Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication
Active sitei643 – 6431Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation
Sitei644 – 6441Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication
Sitei744 – 7441Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication
Binding sitei1229 – 12291NADP 1By similarity
Active sitei1264 – 12641Acyl-ester intermediate; for beta-ketoacyl reductase 1 activityBy similarity
Active sitei1661 – 16611Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation
Active sitei2112 – 21121Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation
Binding sitei2666 – 26661NADP 2Curated
Active sitei2701 – 27011Acyl-ester intermediate; for beta-ketoacyl reductase 2 activityCurated
Binding sitei2965 – 29651SubstrateBy similarity
Active sitei3031 – 30311Nucleophile; for thioesterase activityBy similarity2 Publications
Binding sitei3032 – 30321Substrate; via amide nitrogen1 Publication
Binding sitei3058 – 30581Substrate1 Publication
Active sitei3148 – 31481Proton acceptor; for thioesterase activityBy similarity2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1125 – 11284NADP 1By similarity
Nucleotide bindingi1148 – 11514NADP 1By similarity
Nucleotide bindingi1177 – 11782NADP 1By similarity
Nucleotide bindingi1249 – 12502NADP 1By similarity
Nucleotide bindingi2565 – 25684NADP 2Curated
Nucleotide bindingi2588 – 25914NADP 2Curated
Nucleotide bindingi2617 – 26182NADP 2Curated
Nucleotide bindingi2686 – 26872NADP 2Curated

GO - Molecular functioni

  • cofactor binding Source: InterPro
  • erythronolide synthase activity Source: UniProtKB
  • hydrolase activity, acting on ester bonds 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-17079.
BRENDAi2.3.1.94. 5518.
UniPathwayiUPA00240.

Protein family/group databases

ESTHERisacer-ery3. Thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
6-deoxyerythronolide-B synthase EryA3, modules 5 and 6Curated (EC:2.3.1.941 Publication)
Short name:
DEBS 31 Publication
Alternative name(s):
6-deoxyerythronolide B synthase III1 Publication
Erythronolide synthase
ORF C1 Publication
Gene namesi
Name:eryA1 Publication
OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifieri1836 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeSaccharopolyspora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 317231716-deoxyerythronolide-B synthase EryA3, modules 5 and 6PRO_0000180295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1427 – 14271O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei2854 – 28541O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Homodimer (PubMed:11752428, PubMed:12379102, PubMed:16844787). 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

Protein-protein interaction databases

DIPiDIP-61229N.
STRINGi405948.SeryN2_010100034465.

Structurei

Secondary structure

1
3172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3829Combined sources
Beta strandi41 – 5010Combined sources
Turni51 – 533Combined sources
Helixi57 – 659Combined sources
Helixi76 – 783Combined sources
Beta strandi88 – 903Combined sources
Turni93 – 964Combined sources
Helixi101 – 1033Combined sources
Helixi107 – 1126Combined sources
Helixi115 – 13016Combined sources
Helixi135 – 1384Combined sources
Beta strandi143 – 1497Combined sources
Helixi163 – 1686Combined sources
Helixi169 – 1735Combined sources
Helixi175 – 18612Combined sources
Beta strandi192 – 1965Combined sources
Helixi198 – 2003Combined sources
Helixi201 – 21414Combined sources
Beta strandi219 – 2279Combined sources
Helixi233 – 2386Combined sources
Beta strandi265 – 2739Combined sources
Helixi274 – 2796Combined sources
Beta strandi286 – 29510Combined sources
Beta strandi300 – 3034Combined sources
Helixi307 – 32115Combined sources
Helixi325 – 3273Combined sources
Beta strandi330 – 3323Combined sources
Helixi341 – 35010Combined sources
Turni351 – 3555Combined sources
Beta strandi364 – 3663Combined sources
Helixi369 – 3724Combined sources
Helixi376 – 3783Combined sources
Helixi381 – 39313Combined sources
Beta strandi433 – 4397Combined sources
Beta strandi443 – 45210Combined sources
Beta strandi468 – 4769Combined sources
Helixi477 – 49317Combined sources
Helixi499 – 50810Combined sources
Beta strandi514 – 5229Combined sources
Helixi523 – 53412Combined sources
Beta strandi542 – 5465Combined sources
Beta strandi554 – 5585Combined sources
Helixi570 – 5756Combined sources
Helixi577 – 59014Combined sources
Helixi591 – 5933Combined sources
Helixi598 – 6036Combined sources
Helixi611 – 63121Combined sources
Beta strandi637 – 6415Combined sources
Helixi645 – 6528Combined sources
Helixi658 – 67114Combined sources
Helixi672 – 6754Combined sources
Beta strandi680 – 6867Combined sources
Helixi688 – 6958Combined sources
Helixi696 – 6983Combined sources
Beta strandi701 – 7099Combined sources
Beta strandi714 – 7185Combined sources
Helixi722 – 73312Combined sources
Beta strandi737 – 7415Combined sources
Helixi749 – 7546Combined sources
Helixi755 – 7617Combined sources
Beta strandi771 – 7744Combined sources
Turni777 – 7793Combined sources
Helixi785 – 7873Combined sources
Helixi790 – 7989Combined sources
Helixi803 – 81210Combined sources
Beta strandi817 – 8204Combined sources
Beta strandi822 – 8243Combined sources
Helixi828 – 83811Combined sources
Beta strandi846 – 8483Combined sources
Helixi858 – 86912Combined sources
Turni870 – 8723Combined sources
Helixi878 – 8803Combined sources
Helixi2906 – 291611Combined sources
Helixi2920 – 293112Combined sources
Beta strandi2939 – 29424Combined sources
Beta strandi2948 – 29514Combined sources
Beta strandi2954 – 29563Combined sources
Beta strandi2958 – 29625Combined sources
Beta strandi2966 – 29683Combined sources
Helixi2971 – 29744Combined sources
Helixi2975 – 29817Combined sources
Turni2982 – 29843Combined sources
Beta strandi2987 – 29904Combined sources
Beta strandi3001 – 30044Combined sources
Helixi3005 – 302016Combined sources
Beta strandi3021 – 30233Combined sources
Beta strandi3025 – 30306Combined sources
Helixi3032 – 304615Combined sources
Beta strandi3052 – 30587Combined sources
Turni3062 – 30643Combined sources
Helixi3066 – 30705Combined sources
Helixi3072 – 308110Combined sources
Helixi3089 – 310416Combined sources
Beta strandi3114 – 31218Combined sources
Beta strandi3127 – 31293Combined sources
Beta strandi3136 – 31383Combined sources
Beta strandi3140 – 31467Combined sources
Helixi3150 – 31523Combined sources
Turni3153 – 31553Combined sources
Helixi3156 – 316712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEZX-ray2.80A/B/C2893-3172[»]
1MO2X-ray3.00A/B2893-3172[»]
1PZRNMR-A/B1-39[»]
2HG4X-ray2.73A/B/C/D/E/F1-917[»]
5D3KX-ray1.70A2904-3172[»]
5D3ZX-ray2.10A2904-3172[»]
ProteinModelPortaliQ03133.
SMRiQ03133. Positions 1-901, 2904-3170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03133.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1394 – 146471Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini2821 – 289171Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 14641424Module 5CuratedAdd
BLAST
Regioni41 – 455415Beta-ketoacyl synthase 1CuratedAdd
BLAST
Regioni557 – 874318Acyltransferase 1CuratedAdd
BLAST
Regioni1117 – 1294178Beta-ketoacyl reductase 1CuratedAdd
BLAST
Regioni1492 – 28911400Module 6CuratedAdd
BLAST
Regioni1492 – 1919428Beta-ketoacyl synthase 2CuratedAdd
BLAST
Regioni2022 – 2331310Acyltransferase 2CuratedAdd
BLAST
Regioni2557 – 2731175Beta-ketoacyl reductase 2CuratedAdd
BLAST
Regioni2960 – 3166207ThioesteraseCuratedAdd
BLAST

Sequence similaritiesi

Contains 2 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4107SQU. Bacteria.
COG3321. LUCA.

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.1820. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. 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.
IPR020802. PKS_thioesterase.
IPR015083. Polyketide_synth_docking.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF08990. 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.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF51735. SSF51735. 4 hits.
SSF52151. SSF52151. 4 hits.
SSF53474. SSF53474. 2 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.

Q03133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDNGMTEE KLRRYLKRTV TELDSVTARL REVEHRAGEP IAIVGMACRF
60 70 80 90 100
PGDVDSPESF WEFVSGGGDA IAEAPADRGW EPDPDARLGG MLAAAGDFDA
110 120 130 140 150
GFFGISPREA LAMDPQQRIM LEISWEALER AGHDPVSLRG SATGVFTGVG
160 170 180 190 200
TVDYGPRPDE APDEVLGYVG TGTASSVASG RVAYCLGLEG PAMTVDTACS
210 220 230 240 250
SGLTALHLAM ESLRRDECGL ALAGGVTVMS SPGAFTEFRS QGGLAADGRC
260 270 280 290 300
KPFSKAADGF GLAEGAGVLV LQRLSAARRE GRPVLAVLAG SAVNQDGASN
310 320 330 340 350
GLTAPSGPAQ QRVIRRALEN AGVRAGDVDY VEAHGTGTRL GDPIEVHALL
360 370 380 390 400
STYGAERDPD DPLWIGSVKS NIGHTQAAAG VAGVMKAVLA LRHGEMPRTL
410 420 430 440 450
HFDEPSPQIE WDLGAVSVVS QARSWPAGER PRRAGVSSFG ISGTNAHVIV
460 470 480 490 500
EEAPEADEPE PAPDSGPVPL VLSGRDEQAM RAQAGRLADH LAPEPRNSLR
510 520 530 540 550
DTGFTLATRA SAMEHRAVVV GDRDEALAGL RAVADRRIAD RTATGQGPNS
560 570 580 590 600
PRRVAMVFPG QGAQWQGMAR DLLRESQVFA DSIRDCERAL APHVDWSLTD
610 620 630 640 650
LLSGARPLDR VDVVQPALFA VMVSLAALWR SHGVEPAAVV GHSQGEIAAA
660 670 680 690 700
HVAGALTLED AAKLVAVRSR VLRRLGGQGG MASFGLGTEQ AAERIGRFAG
710 720 730 740 750
ALSIASVNGP RSVVVVAGES GPLDELIAEC EAEAHKARRI PVDYASHSPQ
760 770 780 790 800
VESLREELLT ELAGISPVSA DVALYSTTTG QPIDTATMDT AYWYANLREQ
810 820 830 840 850
VRFQDATRQL AEAGFDAFVE VSPHPVLTVG IEATLDSALP ADAGACVVGT
860 870 880 890 900
LRRDRGGLAD FHTALGEAYA QGVEVDWSPA FADARPVELP VYPFQRYWLP
910 920 930 940 950
IPTGGRARDE DDDWRYQVVW REAEWESASL AGRVLLVTGP GVPSELSDAI
960 970 980 990 1000
RSGLEQSGAT VLTCDVESRS TIGTALEAAD TDALSTVGVA AVPHGEAVDP
1010 1020 1030 1040 1050
SLDALALVQA LGAAGVEAPL WVLTRNAVQV ADGELVDPAQ AMVGGLGRVV
1060 1070 1080 1090 1100
GIEQPGRWGG LVDLVDADAA SIRSLAAVLA DPRGEEQVAI RADGIKVARL
1110 1120 1130 1140 1150
VPAPARARTH PLEPLAGTVL VTGGTGGIGA HLARWLARSG AEHLVLLGRR
1160 1170 1180 1190 1200
GADAPGASEL REELTALGTG VTIAACDVAD RARLEAVLAA EAAAEGRTVS
1210 1220 1230 1240 1250
AVMHAAGVST STPLDDLTEA EFTEIADVKV RGTVNLDELC PDLDAFVLFS
1260 1270 1280 1290 1300
SNAGVWGSPG LASYAAANAF LDGFARAARS EGAPVTSIAW GLWAGQNMAG
1310 1320 1330 1340 1350
DEGGEYLRSQ GLRAMDPDRA VEELHITLDH GQTSVSVVDM DRRRFVELFT
1360 1370 1380 1390 1400
AARHRPLFDE IAGARAEARQ SEEGPALAQR LAALLCDGRE REHLAHLIRA
1410 1420 1430 1440 1450
EVAAVLGHGD DAAIDRDRAF RDLGFDSMTA VDLRNRLAAV TGVREAATVV
1460 1470 1480 1490 1500
FDHPTITRLA DHYLERLVGA AEAEQAPALV REVPPKDADD PIAIVGMACR
1510 1520 1530 1540 1550
FPGGVHNPGE LWEFIVGGGD AVTEMPTDRG WDLDALFDPD PQRHGTSYSR
1560 1570 1580 1590 1600
HGAFLDGAAD FDAAFFGISP REALAMDPQQ RQVLETTWEL FENAGIDPHS
1610 1620 1630 1640 1650
VRGSDTGVFL GAAYQGYGQD AVVPEDSEGY LLTGNSSAVV SGRVAYVLGL
1660 1670 1680 1690 1700
EGPAVTVDTA CSSSLVALHS ACGSLRDGDC GLAVAGGVSV MAGPEVFTEF
1710 1720 1730 1740 1750
SRQGGLAVDG RCKAFSAEAD GFGLPEGVAV VQLQRLSDGP AEGGRQVLGV
1760 1770 1780 1790 1800
VAGSAINQDG ATNGLAAPSG VAQQRVIRKA WARAGITGAD VAVVEAHGTG
1810 1820 1830 1840 1850
TRLGDPVEAS ALLATYGKSR GSSGPVLLGS VKSNIGHAQA AAGVAGVIKV
1860 1870 1880 1890 1900
VLGLNRGLVP PMLCRGERSP LIEWSSGGVE LAEAVSPWPP AADGVRRAGV
1910 1920 1930 1940 1950
SAFGVSGTNA HVIIAEPPEP EPLPEPGPVG VLAAANSVPV LLSARTETAL
1960 1970 1980 1990 2000
AAQARLLESA VDDSVPLTAL ASALATGRAH LPRRAALLAG DHEQLRGQLR
2010 2020 2030 2040 2050
AVAEGVAAPG ATTGTASAGG VVFVFPGQGA QWEGMARGLL SVPVFAESIA
2060 2070 2080 2090 2100
ECDAVLSEVA GFSASEVLEQ RPDAPSLERV DVVQPVLFSV MVSLARLWGA
2110 2120 2130 2140 2150
CGVSPSAVIG HSQGEIAAAV VAGVLSLEDG VRVVALRAKA LRALAGKGGM
2160 2170 2180 2190 2200
VSLAAPGERA RALIAPWEDR ISVAAVNSPS SVVVSGDPEA LAELVARCED
2210 2220 2230 2240 2250
EGVRAKTLPV DYASHSRHVE EIRETILADL DGISARRAAI PLYSTLHGER
2260 2270 2280 2290 2300
RDMGPRYWYD NLRSQVRFDE AVSAQSPDGH ATFVEMSPHP VLTAAVQEIA
2310 2320 2330 2340 2350
ADAVAIGSLH RDTAEEHLIA ELARAHVHGV AVDWRNVFPA APPVALPNYP
2360 2370 2380 2390 2400
FEPQRYWLAP EVSDQLADSR YRVDWRPLAT TPVDLEGGFL VHGSAPESLT
2410 2420 2430 2440 2450
SAVEKAGGVV PVASADREAL AAALREVPGE VAGVLSVHTG AANALALHQS
2460 2470 2480 2490 2500
LGEAGVRAPL WLVTSRAVAL GESEPVDPEQ AMVWGLGRVM GLETPERWGG
2510 2520 2530 2540 2550
LVDLPAEPAP GDGEAFVACL GADGHEDQVA IRDHARYGRR LVRAPLGTRE
2560 2570 2580 2590 2600
SSWEPAGTAL VTGGTGALGG HVARHLARCG VEDLVLVSRR GVDAPAAAEL
2610 2620 2630 2640 2650
EAELVALGPK TTITACDVAD REQLSKLLEE LRGQGRPVRT VVHTAGVPES
2660 2670 2680 2690 2700
RPLHEIGELE SVCAAKVTGA RLLDELCPDA ETFVLFSSGA GVWGSANLGA
2710 2720 2730 2740 2750
YSAANAYLDA LAHRRRAEGR AATSVAWGAW AGEGMATGDL EGLTRRGLRP
2760 2770 2780 2790 2800
MAPDRAIRAL HQALDNGDTC VSIADVDWEA FAVGFTAARP RPLLDELVTP
2810 2820 2830 2840 2850
AVGAVPAVQA APAREMTSQE LLEFTHSHVA AILGHSSPDA VGQDQPFTEL
2860 2870 2880 2890 2900
GFDSLTAVGL RNQLQQATGL ALPATLVFEH PTVRRLADHI GQQLDSGTPA
2910 2920 2930 2940 2950
REASSALRDG YRQAGVSGRV RSYLDLLAGL SDFREHFDGS DGFSLDLVDM
2960 2970 2980 2990 3000
ADGPGEVTVI CCAGTAAISG PHEFTRLAGA LRGIAPVRAV PQPGYEEGEP
3010 3020 3030 3040 3050
LPSSMAAVAA VQADAVIRTQ GDKPFVVAGH SAGALMAYAL ATELLDRGHP
3060 3070 3080 3090 3100
PRGVVLIDVY PPGHQDAMNA WLEELTATLF DRETVRMDDT RLTALGAYDR
3110 3120 3130 3140 3150
LTGQWRPRET GLPTLLVSAG EPMGPWPDDS WKPTWPFEHD TVAVPGDHFT
3160 3170
MVQEHADAIA RHIDAWLGGG NS
Length:3,172
Mass (Da):331,479
Last modified:January 23, 2007 - v4
Checksum:iDBBD5094E77DDD5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891A → R in AAA26495 (PubMed:2024119).Curated
Sequence conflicti493 – 51725PEPRN…MEHRA → ASRGTRCATPVSRWPPAAAP WEQ in CAA39583 (PubMed:2234082).CuratedAdd
BLAST
Sequence conflicti493 – 4931P → R in AAA26495 (PubMed:2024119).Curated
Sequence conflicti510 – 5101A → R in AAA26495 (PubMed:2024119).Curated
Sequence conflicti513 – 5131M → W in AAA26495 (PubMed:2024119).Curated
Sequence conflicti525 – 5251E → D in AAA26495 (PubMed:2024119).Curated
Sequence conflicti536 – 5361R → G in AAA26495 (PubMed:2024119).Curated
Sequence conflicti547 – 5515GPNSP → ARTR in AAA26495 (PubMed:2024119).Curated
Sequence conflicti673 – 6731R → A in AAA26495 (PubMed:2024119).Curated
Sequence conflicti716 – 7161Missing in AAA26495 (PubMed:2024119).Curated
Sequence conflicti734 – 7363AHK → GIT in AAA26495 (PubMed:2024119).Curated
Sequence conflicti896 – 8961R → RELPVYPFQRQR in CAA39583 (PubMed:2234082).Curated
Sequence conflicti896 – 8961R → RQR in AAA26495 (PubMed:2024119).Curated
Sequence conflicti988 – 9947GVAAVPH → VSLLSRD in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1108 – 11169RTHPLEPLA → ARTRWSPR in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1123 – 11253Missing in CAA39583 (PubMed:2234082).Curated
Sequence conflicti1132 – 11321L → V in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1192 – 11921A → R in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1194 – 11941Missing in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1277 – 12782AA → RR in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1385 – 13906LCDGRE → STAER in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1485 – 14851Missing in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1518 – 15181G → R in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1601 – 16011V → L in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1724 – 17252LP → FA in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1732 – 17321Q → L in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1739 – 17435GPAEG → ARRA in AAA26495 (PubMed:2024119).Curated
Sequence conflicti1762 – 17621T → S in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2252 – 22521D → DGAD in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2275 – 22773QSP → AVA in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2408 – 24081G → GR in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2420 – 24212LA → S in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2443 – 24442NA → TH in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2596 – 25961A → G in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2609 – 26091P → A in AAA26495 (PubMed:2024119).Curated
Sequence conflicti2715 – 27228RRAEGRAA → AVRKAVRR in CAA39583 (PubMed:2234082).Curated
Sequence conflicti2754 – 27541D → E in AAA26495 (PubMed:2024119).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56107 Genomic DNA. Translation: CAA39583.1.
M63677 Genomic DNA. Translation: AAA26495.1.
X62569 Genomic DNA. Translation: CAA44449.1.
PIRiS13595.
S22012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56107 Genomic DNA. Translation: CAA39583.1.
M63677 Genomic DNA. Translation: AAA26495.1.
X62569 Genomic DNA. Translation: CAA44449.1.
PIRiS13595.
S22012.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEZX-ray2.80A/B/C2893-3172[»]
1MO2X-ray3.00A/B2893-3172[»]
1PZRNMR-A/B1-39[»]
2HG4X-ray2.73A/B/C/D/E/F1-917[»]
5D3KX-ray1.70A2904-3172[»]
5D3ZX-ray2.10A2904-3172[»]
ProteinModelPortaliQ03133.
SMRiQ03133. Positions 1-901, 2904-3170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61229N.
STRINGi405948.SeryN2_010100034465.

Protein family/group databases

ESTHERisacer-ery3. Thioesterase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107SQU. Bacteria.
COG3321. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00240.
BioCyciMetaCyc:MONOMER-17079.
BRENDAi2.3.1.94. 5518.

Miscellaneous databases

EvolutionaryTraceiQ03133.

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.1820. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. 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.
IPR020802. PKS_thioesterase.
IPR015083. Polyketide_synth_docking.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF08990. 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.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF51735. SSF51735. 4 hits.
SSF52151. SSF52151. 4 hits.
SSF53474. SSF53474. 2 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 nameiERYA3_SACER
AccessioniPrimary (citable) accession number: Q03133
Secondary accession number(s): Q54097, Q99270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 131 of the entry and version 4 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

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.