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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)DescriptionActionsGraphical viewLength
Active sitei199Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication1
Active sitei643Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation1
Sitei644Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication1
Sitei744Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication1
Binding sitei1229NADP 1By similarity1
Active sitei1264Acyl-ester intermediate; for beta-ketoacyl reductase 1 activityBy similarity1
Active sitei1661Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1
Active sitei2112Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation1
Binding sitei2666NADP 2Curated1
Active sitei2701Acyl-ester intermediate; for beta-ketoacyl reductase 2 activityCurated1
Binding sitei2965SubstrateBy similarity1
Active sitei3031Nucleophile; for thioesterase activityBy similarity2 Publications1
Binding sitei3032Substrate; via amide nitrogen1 Publication1
Binding sitei3058Substrate1 Publication1
Active sitei3148Proton acceptor; for thioesterase activityBy similarity2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1125 – 1128NADP 1By similarity4
Nucleotide bindingi1148 – 1151NADP 1By similarity4
Nucleotide bindingi1177 – 1178NADP 1By similarity2
Nucleotide bindingi1249 – 1250NADP 1By similarity2
Nucleotide bindingi2565 – 2568NADP 2Curated4
Nucleotide bindingi2588 – 2591NADP 2Curated4
Nucleotide bindingi2617 – 2618NADP 2Curated2
Nucleotide bindingi2686 – 2687NADP 2Curated2

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001802952 – 31726-deoxyerythronolide-B synthase EryA3, modules 5 and 6Add BLAST3171

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1427O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2854O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

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

13172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 38Combined sources29
Beta strandi41 – 50Combined sources10
Turni51 – 53Combined sources3
Helixi57 – 65Combined sources9
Helixi76 – 78Combined sources3
Beta strandi88 – 90Combined sources3
Turni93 – 96Combined sources4
Helixi101 – 103Combined sources3
Helixi107 – 112Combined sources6
Helixi115 – 130Combined sources16
Helixi135 – 138Combined sources4
Beta strandi143 – 149Combined sources7
Helixi163 – 168Combined sources6
Helixi169 – 173Combined sources5
Helixi175 – 186Combined sources12
Beta strandi192 – 196Combined sources5
Helixi198 – 200Combined sources3
Helixi201 – 214Combined sources14
Beta strandi219 – 227Combined sources9
Helixi233 – 238Combined sources6
Beta strandi265 – 273Combined sources9
Helixi274 – 279Combined sources6
Beta strandi286 – 295Combined sources10
Beta strandi300 – 303Combined sources4
Helixi307 – 321Combined sources15
Helixi325 – 327Combined sources3
Beta strandi330 – 332Combined sources3
Helixi341 – 350Combined sources10
Turni351 – 355Combined sources5
Beta strandi364 – 366Combined sources3
Helixi369 – 372Combined sources4
Helixi376 – 378Combined sources3
Helixi381 – 393Combined sources13
Beta strandi433 – 439Combined sources7
Beta strandi443 – 452Combined sources10
Beta strandi468 – 476Combined sources9
Helixi477 – 493Combined sources17
Helixi499 – 508Combined sources10
Beta strandi514 – 522Combined sources9
Helixi523 – 534Combined sources12
Beta strandi542 – 546Combined sources5
Beta strandi554 – 558Combined sources5
Helixi570 – 575Combined sources6
Helixi577 – 590Combined sources14
Helixi591 – 593Combined sources3
Helixi598 – 603Combined sources6
Helixi611 – 631Combined sources21
Beta strandi637 – 641Combined sources5
Helixi645 – 652Combined sources8
Helixi658 – 671Combined sources14
Helixi672 – 675Combined sources4
Beta strandi680 – 686Combined sources7
Helixi688 – 695Combined sources8
Helixi696 – 698Combined sources3
Beta strandi701 – 709Combined sources9
Beta strandi714 – 718Combined sources5
Helixi722 – 733Combined sources12
Beta strandi737 – 741Combined sources5
Helixi749 – 754Combined sources6
Helixi755 – 761Combined sources7
Beta strandi771 – 774Combined sources4
Turni777 – 779Combined sources3
Helixi785 – 787Combined sources3
Helixi790 – 798Combined sources9
Helixi803 – 812Combined sources10
Beta strandi817 – 820Combined sources4
Beta strandi822 – 824Combined sources3
Helixi828 – 838Combined sources11
Beta strandi846 – 848Combined sources3
Helixi858 – 869Combined sources12
Turni870 – 872Combined sources3
Helixi878 – 880Combined sources3
Helixi2906 – 2916Combined sources11
Helixi2920 – 2931Combined sources12
Beta strandi2939 – 2942Combined sources4
Beta strandi2948 – 2951Combined sources4
Beta strandi2954 – 2956Combined sources3
Beta strandi2958 – 2962Combined sources5
Beta strandi2966 – 2968Combined sources3
Helixi2971 – 2974Combined sources4
Helixi2975 – 2981Combined sources7
Turni2982 – 2984Combined sources3
Beta strandi2987 – 2990Combined sources4
Beta strandi3001 – 3004Combined sources4
Helixi3005 – 3020Combined sources16
Beta strandi3021 – 3023Combined sources3
Beta strandi3025 – 3030Combined sources6
Helixi3032 – 3046Combined sources15
Beta strandi3052 – 3058Combined sources7
Turni3062 – 3064Combined sources3
Helixi3066 – 3070Combined sources5
Helixi3072 – 3081Combined sources10
Helixi3089 – 3104Combined sources16
Beta strandi3114 – 3121Combined sources8
Beta strandi3127 – 3129Combined sources3
Beta strandi3136 – 3138Combined sources3
Beta strandi3140 – 3146Combined sources7
Helixi3150 – 3152Combined sources3
Turni3153 – 3155Combined sources3
Helixi3156 – 3167Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03133.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1394 – 1464Acyl carrier 1PROSITE-ProRule annotationAdd BLAST71
Domaini2821 – 2891Acyl carrier 2PROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 1464Module 5CuratedAdd BLAST1424
Regioni41 – 455Beta-ketoacyl synthase 1CuratedAdd BLAST415
Regioni557 – 874Acyltransferase 1CuratedAdd BLAST318
Regioni1117 – 1294Beta-ketoacyl reductase 1CuratedAdd BLAST178
Regioni1492 – 2891Module 6CuratedAdd BLAST1400
Regioni1492 – 1919Beta-ketoacyl synthase 2CuratedAdd BLAST428
Regioni2022 – 2331Acyltransferase 2CuratedAdd BLAST310
Regioni2557 – 2731Beta-ketoacyl reductase 2CuratedAdd BLAST175
Regioni2960 – 3166ThioesteraseCuratedAdd BLAST207

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)DescriptionActionsGraphical viewLength
Sequence conflicti289A → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti493 – 517PEPRN…MEHRA → ASRGTRCATPVSRWPPAAAP WEQ in CAA39583 (PubMed:2234082).CuratedAdd BLAST25
Sequence conflicti493P → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti510A → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti513M → W in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti525E → D in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti536R → G in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti547 – 551GPNSP → ARTR in AAA26495 (PubMed:2024119).Curated5
Sequence conflicti673R → A in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti716Missing in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti734 – 736AHK → GIT in AAA26495 (PubMed:2024119).Curated3
Sequence conflicti896R → RELPVYPFQRQR in CAA39583 (PubMed:2234082).Curated1
Sequence conflicti896R → RQR in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti988 – 994GVAAVPH → VSLLSRD in AAA26495 (PubMed:2024119).Curated7
Sequence conflicti1108 – 1116RTHPLEPLA → ARTRWSPR in AAA26495 (PubMed:2024119).Curated9
Sequence conflicti1123 – 1125Missing in CAA39583 (PubMed:2234082).Curated3
Sequence conflicti1132L → V in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1192A → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1194Missing in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1277 – 1278AA → RR in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti1385 – 1390LCDGRE → STAER in AAA26495 (PubMed:2024119).Curated6
Sequence conflicti1485Missing in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1518G → R in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1601V → L in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1724 – 1725LP → FA in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti1732Q → L in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti1739 – 1743GPAEG → ARRA in AAA26495 (PubMed:2024119).Curated5
Sequence conflicti1762T → S in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2252D → DGAD in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2275 – 2277QSP → AVA in AAA26495 (PubMed:2024119).Curated3
Sequence conflicti2408G → GR in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2420 – 2421LA → S in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti2443 – 2444NA → TH in AAA26495 (PubMed:2024119).Curated2
Sequence conflicti2596A → G in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2609P → A in AAA26495 (PubMed:2024119).Curated1
Sequence conflicti2715 – 2722RRAEGRAA → AVRKAVRR in CAA39583 (PubMed:2234082).Curated8
Sequence conflicti2754D → E in AAA26495 (PubMed:2024119).Curated1

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
PDB 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.
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: November 2, 2016
This is version 133 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.