UniProtKB - Q03133 (ERYA3_SACER)
6-deoxyerythronolide-B synthase EryA3, modules 5 and 6
eryA
Functioni
Involved in the biosynthesis of antibiotic erythromycin via the biosynthesis of its aglycone precursor, 6-deoxyerythronolide B (6-dEB).
1 Publication1 PublicationMiscellaneous
Catalytic activityi
- 6 (S)-methylmalonyl-CoA + 12 H+ + 6 NADPH + propanoyl-CoA = 6-deoxyerythronolide B + 6 CO2 + 7 CoA + H2O + 6 NADP+1 PublicationEC:2.3.1.941 Publication
Cofactori
Activity regulationi
: erythromycin biosynthesis Pathwayi
This protein is involved in the pathway erythromycin biosynthesis, which is part of Antibiotic biosynthesis.2 PublicationsView all proteins of this organism that are known to be involved in the pathway erythromycin biosynthesis and in Antibiotic biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 199 | Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 643 | Acyl-ester intermediate; for acyltransferase 1 activityPROSITE-ProRule annotation | 1 | |
Sitei | 644 | Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication | 1 | |
Sitei | 744 | Important for discrimination between malonyl and methylmalonyl polyketide chain extension units1 Publication | 1 | |
Binding sitei | 1229 | NADP 1By similarity | 1 | |
Active sitei | 1264 | Acyl-ester intermediate; for beta-ketoacyl reductase 1 activityBy similarity | 1 | |
Active sitei | 1661 | Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2112 | Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 2666 | NADP 2Curated | 1 | |
Active sitei | 2701 | Acyl-ester intermediate; for beta-ketoacyl reductase 2 activityCurated | 1 | |
Binding sitei | 2965 | SubstrateBy similarity | 1 | |
Active sitei | 3031 | Nucleophile; for thioesterase activityBy similarity2 Publications | 1 | |
Binding sitei | 3032 | Substrate; via amide nitrogen1 Publication | 1 | |
Binding sitei | 3058 | Substrate1 Publication | 1 | |
Active sitei | 3148 | Proton acceptor; for thioesterase activityBy similarity2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1125 – 1128 | NADP 1By similarity | 4 | |
Nucleotide bindingi | 1148 – 1151 | NADP 1By similarity | 4 | |
Nucleotide bindingi | 1177 – 1178 | NADP 1By similarity | 2 | |
Nucleotide bindingi | 1249 – 1250 | NADP 1By similarity | 2 | |
Nucleotide bindingi | 2565 – 2568 | NADP 2Curated | 4 | |
Nucleotide bindingi | 2588 – 2591 | NADP 2Curated | 4 | |
Nucleotide bindingi | 2617 – 2618 | NADP 2Curated | 2 | |
Nucleotide bindingi | 2686 – 2687 | NADP 2Curated | 2 |
GO - Molecular functioni
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
- erythronolide synthase activity Source: UniProtKB
- phosphopantetheine binding Source: UniProtKB
GO - Biological processi
- fatty acid biosynthetic process Source: InterPro
- macrolide biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Transferase |
Biological process | Antibiotic biosynthesis |
Ligand | NADP |
Enzyme and pathway databases
BRENDAi | 2.3.1.94, 5518 |
UniPathwayi | UPA00240 |
Protein family/group databases
ESTHERi | sacer-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 |
Organismi | Saccharopolyspora erythraea (Streptomyces erythraeus) |
Taxonomic identifieri | 1836 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Pseudonocardiales › Pseudonocardiaceae › Saccharopolyspora |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000180295 | 2 – 3172 | 6-deoxyerythronolide-B synthase EryA3, modules 5 and 6Add BLAST | 3171 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1427 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 | |
Modified residuei | 2854 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinProteomic databases
PRIDEi | Q03133 |
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 PublicationsProtein-protein interaction databases
DIPi | DIP-61229N |
Structurei
Secondary structure
3D structure databases
SMRi | Q03133 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q03133 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1392 – 1467 | Carrier 1PROSITE-ProRule annotationAdd BLAST | 76 | |
Domaini | 2819 – 2894 | Carrier 2PROSITE-ProRule annotationAdd BLAST | 76 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 41 – 1464 | Module 5CuratedAdd BLAST | 1424 | |
Regioni | 41 – 455 | Beta-ketoacyl synthase 1CuratedAdd BLAST | 415 | |
Regioni | 557 – 874 | Acyltransferase 1CuratedAdd BLAST | 318 | |
Regioni | 1117 – 1294 | Beta-ketoacyl reductase 1CuratedAdd BLAST | 178 | |
Regioni | 1492 – 2891 | Module 6CuratedAdd BLAST | 1400 | |
Regioni | 1492 – 1919 | Beta-ketoacyl synthase 2CuratedAdd BLAST | 428 | |
Regioni | 2022 – 2331 | Acyltransferase 2CuratedAdd BLAST | 310 | |
Regioni | 2557 – 2731 | Beta-ketoacyl reductase 2CuratedAdd BLAST | 175 | |
Regioni | 2960 – 3166 | ThioesteraseCuratedAdd BLAST | 207 |
Keywords - Domaini
RepeatFamily and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.40.366.10, 2 hits 3.40.47.10, 2 hits 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR013968, PKS_KR IPR020806, PKS_PP-bd IPR020802, PKS_thioesterase IPR015083, Polyketide_synth_docking IPR036299, Polyketide_synth_docking_sf IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site IPR001031, Thioesterase IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF00698, 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 |
SMARTi | View protein in SMART SM00827, PKS_AT, 2 hits SM00825, PKS_KS, 2 hits SM00823, PKS_PP, 2 hits SM00824, PKS_TE, 1 hit |
SUPFAMi | SSF101173, SSF101173, 1 hit SSF47336, SSF47336, 2 hits SSF51735, SSF51735, 4 hits SSF52151, SSF52151, 2 hits SSF53474, SSF53474, 1 hit SSF53901, SSF53901, 2 hits SSF55048, SSF55048, 2 hits |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 2 hits PS50075, CARRIER, 2 hits PS00012, PHOSPHOPANTETHEINE, 2 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 289 | A → R in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 493 – 517 | PEPRN…MEHRA → ASRGTRCATPVSRWPPAAAP WEQ in CAA39583 (PubMed:2234082).CuratedAdd BLAST | 25 | |
Sequence conflicti | 493 | P → R in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 510 | A → R in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 513 | M → W in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 525 | E → D in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 536 | R → G in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 547 – 551 | GPNSP → ARTR in AAA26495 (PubMed:2024119).Curated | 5 | |
Sequence conflicti | 673 | R → A in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 716 | Missing in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 734 – 736 | AHK → GIT in AAA26495 (PubMed:2024119).Curated | 3 | |
Sequence conflicti | 896 | R → RELPVYPFQRQR in CAA39583 (PubMed:2234082).Curated | 1 | |
Sequence conflicti | 896 | R → RQR in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 988 – 994 | GVAAVPH → VSLLSRD in AAA26495 (PubMed:2024119).Curated | 7 | |
Sequence conflicti | 1108 – 1116 | RTHPLEPLA → ARTRWSPR in AAA26495 (PubMed:2024119).Curated | 9 | |
Sequence conflicti | 1123 – 1125 | Missing in CAA39583 (PubMed:2234082).Curated | 3 | |
Sequence conflicti | 1132 | L → V in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1192 | A → R in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1194 | Missing in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1277 – 1278 | AA → RR in AAA26495 (PubMed:2024119).Curated | 2 | |
Sequence conflicti | 1385 – 1390 | LCDGRE → STAER in AAA26495 (PubMed:2024119).Curated | 6 | |
Sequence conflicti | 1485 | Missing in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1518 | G → R in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1601 | V → L in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1724 – 1725 | LP → FA in AAA26495 (PubMed:2024119).Curated | 2 | |
Sequence conflicti | 1732 | Q → L in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 1739 – 1743 | GPAEG → ARRA in AAA26495 (PubMed:2024119).Curated | 5 | |
Sequence conflicti | 1762 | T → S in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 2252 | D → DGAD in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 2275 – 2277 | QSP → AVA in AAA26495 (PubMed:2024119).Curated | 3 | |
Sequence conflicti | 2408 | G → GR in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 2420 – 2421 | LA → S in AAA26495 (PubMed:2024119).Curated | 2 | |
Sequence conflicti | 2443 – 2444 | NA → TH in AAA26495 (PubMed:2024119).Curated | 2 | |
Sequence conflicti | 2596 | A → G in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 2609 | P → A in AAA26495 (PubMed:2024119).Curated | 1 | |
Sequence conflicti | 2715 – 2722 | RRAEGRAA → AVRKAVRR in CAA39583 (PubMed:2234082).Curated | 8 | |
Sequence conflicti | 2754 | D → E in AAA26495 (PubMed:2024119).Curated | 1 |
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 |
PIRi | S13595 S22012 |
Similar proteinsi
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 |
PIRi | S13595 S22012 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KEZ | X-ray | 2.80 | A/B/C | 2893-3172 | [»] | |
1MO2 | X-ray | 3.00 | A/B | 2893-3172 | [»] | |
1PZR | NMR | - | A/B | 1-39 | [»] | |
2HG4 | X-ray | 2.73 | A/B/C/D/E/F | 1-917 | [»] | |
5D3K | X-ray | 1.70 | A | 2904-3172 | [»] | |
5D3Z | X-ray | 2.10 | A | 2904-3172 | [»] | |
6MLK | X-ray | 2.45 | A | 2893-3172 | [»] | |
7M7E | electron microscopy | 3.20 | A/B | 2896-3172 | [»] | |
7M7F | electron microscopy | 3.20 | A/B | 2896-3172 | [»] | |
7M7G | electron microscopy | 4.10 | A/B | 2896-3172 | [»] | |
7M7H | electron microscopy | 4.10 | A/B | 2896-3172 | [»] | |
SMRi | Q03133 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-61229N |
Protein family/group databases
ESTHERi | sacer-ery3, Thioesterase |
Proteomic databases
PRIDEi | Q03133 |
Protocols and materials databases
ABCDi | Q03133, 1 sequenced antibody |
Enzyme and pathway databases
UniPathwayi | UPA00240 |
BRENDAi | 2.3.1.94, 5518 |
Miscellaneous databases
EvolutionaryTracei | Q03133 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.40.366.10, 2 hits 3.40.47.10, 2 hits 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR013968, PKS_KR IPR020806, PKS_PP-bd IPR020802, PKS_thioesterase IPR015083, Polyketide_synth_docking IPR036299, Polyketide_synth_docking_sf IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site IPR001031, Thioesterase IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF00698, 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 |
SMARTi | View protein in SMART SM00827, PKS_AT, 2 hits SM00825, PKS_KS, 2 hits SM00823, PKS_PP, 2 hits SM00824, PKS_TE, 1 hit |
SUPFAMi | SSF101173, SSF101173, 1 hit SSF47336, SSF47336, 2 hits SSF51735, SSF51735, 4 hits SSF52151, SSF52151, 2 hits SSF53474, SSF53474, 1 hit SSF53901, SSF53901, 2 hits SSF55048, SSF55048, 2 hits |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 2 hits PS50075, CARRIER, 2 hits PS00012, PHOSPHOPANTETHEINE, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ERYA3_SACER | |
Accessioni | Q03133Primary (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: | May 25, 2022 | |
This is version 153 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references