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Q03133

- ERYA3_SACER

UniProt

Q03133 - ERYA3_SACER

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Protein

Erythronolide synthase, modules 5 and 6

Gene

eryA

Organism
Saccharopolyspora erythraea (Streptomyces erythraeus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+.

Cofactori

Binds 2 phosphopantetheines covalently.
NADP.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei199 – 1991Acyl-thioester intermediatePROSITE-ProRule annotation
Active sitei643 – 6431Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei1661 – 16611Acyl-thioester intermediatePROSITE-ProRule annotation
Active sitei2112 – 21121Acyl-ester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1118 – 116447NADPAdd
BLAST
Nucleotide bindingi2557 – 260549NADPAdd
BLAST

GO - Molecular functioni

  1. cofactor binding Source: InterPro
  2. erythronolide synthase activity Source: UniProtKB-EC
  3. hydrolase activity, acting on ester bonds Source: InterPro
  4. oxidoreductase activity Source: InterPro
  5. phosphopantetheine binding Source: InterPro

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17079.
UniPathwayiUPA00240.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythronolide synthase, modules 5 and 6 (EC:2.3.1.94)
Alternative name(s):
6-deoxyerythronolide B synthase III
DEBS 3
ORF 3
Gene namesi
Name:eryA
OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifieri1836 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 31723171Erythronolide synthase, 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

Structurei

Secondary structure

1
3172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3829
Beta strandi41 – 5010
Turni51 – 533
Helixi57 – 659
Helixi76 – 783
Beta strandi88 – 903
Turni93 – 964
Helixi101 – 1033
Helixi107 – 1126
Helixi115 – 13016
Helixi135 – 1384
Beta strandi143 – 1497
Helixi163 – 1686
Helixi169 – 1735
Helixi175 – 18612
Beta strandi192 – 1965
Helixi198 – 2003
Helixi201 – 21414
Beta strandi219 – 2279
Helixi233 – 2386
Beta strandi265 – 2739
Helixi274 – 2796
Beta strandi286 – 29510
Beta strandi300 – 3034
Helixi307 – 32115
Helixi325 – 3273
Beta strandi330 – 3323
Helixi341 – 35010
Turni351 – 3555
Beta strandi364 – 3663
Helixi369 – 3724
Helixi376 – 3783
Helixi381 – 39313
Beta strandi433 – 4397
Beta strandi443 – 45210
Beta strandi468 – 4769
Helixi477 – 49317
Helixi499 – 50810
Beta strandi514 – 5229
Helixi523 – 53412
Beta strandi542 – 5465
Beta strandi554 – 5585
Helixi570 – 5756
Helixi577 – 59014
Helixi591 – 5933
Helixi598 – 6036
Helixi611 – 63121
Beta strandi637 – 6415
Helixi645 – 6528
Helixi658 – 67114
Helixi672 – 6754
Beta strandi680 – 6867
Helixi688 – 6958
Helixi696 – 6983
Beta strandi701 – 7099
Beta strandi714 – 7185
Helixi722 – 73312
Beta strandi737 – 7415
Helixi749 – 7546
Helixi755 – 7617
Beta strandi771 – 7744
Turni777 – 7793
Helixi785 – 7873
Helixi790 – 7989
Helixi803 – 81210
Beta strandi817 – 8204
Beta strandi822 – 8243
Helixi828 – 83811
Beta strandi846 – 8483
Helixi858 – 86912
Turni870 – 8723
Helixi878 – 8803
Helixi2909 – 29179
Helixi2921 – 293111
Beta strandi2938 – 29414
Beta strandi2948 – 29514
Beta strandi2956 – 29616
Beta strandi2966 – 29683
Turni2971 – 29744
Helixi2975 – 29806
Beta strandi2982 – 29843
Beta strandi2987 – 29904
Beta strandi3001 – 30044
Helixi3005 – 301915
Beta strandi3021 – 30233
Beta strandi3025 – 30284
Helixi3032 – 304312
Turni3044 – 30485
Beta strandi3052 – 30554
Turni3062 – 30643
Helixi3066 – 307611
Helixi3077 – 30793
Helixi3089 – 310113
Turni3102 – 31043
Beta strandi3114 – 31218
Beta strandi3140 – 31467
Turni3148 – 31503
Beta strandi3151 – 31544
Helixi3157 – 316711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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
Regioni2 – 14841483Module 5Add
BLAST
Regioni37 – 484448Beta-ketoacyl synthase 1Add
BLAST
Regioni554 – 878325Acyltransferase (AT) 1Add
BLAST
Regioni1116 – 1298183Beta-ketoacyl reductase 1Add
BLAST
Regioni1485 – 31721688Module 6Add
BLAST
Regioni1488 – 1954467Beta-ketoacyl synthase 2Add
BLAST
Regioni2021 – 2335315Acyltransferase (AT) 2Add
BLAST
Regioni2555 – 2735181Beta-ketoacyl reductase 2Add
BLAST
Regioni2926 – 3172247ThioesteraseAdd
BLAST

Sequence similaritiesi

Contains 2 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.1820. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR002198. DH_sc/Rdtase_SDR.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF00106. adh_short. 2 hits.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF00550. PP-binding. 2 hits.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00822. PKS_KR. 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.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q03133.
SMRi Q03133. Positions 1-901, 2904-3170.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00240 .
BioCyci MetaCyc:MONOMER-17079.

Miscellaneous databases

EvolutionaryTracei Q03133.

Family and domain databases

Gene3Di 1.10.1200.10. 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.
InterProi IPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR002198. DH_sc/Rdtase_SDR.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 2 hits.
PF00106. adh_short. 2 hits.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF00550. PP-binding. 2 hits.
PF00975. Thioesterase. 1 hit.
[Graphical view ]
SMARTi SM00827. PKS_AT. 2 hits.
SM00822. PKS_KR. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view ]
SUPFAMi SSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF52151. SSF52151. 4 hits.
SSF53474. SSF53474. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 2 hits.
PROSITEi PS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea."
    Cortes J., Haydock S.F., Roberts G.A., Bevitt D.J., Leadlay P.F.
    Nature 348:176-178(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11635 / DSM 40517 / IFO 13426 / JCM 4026 / NCIB 8594.
  2. "Modular organization of genes required for complex polyketide biosynthesis."
    Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L.
    Science 252:675-679(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "6-deoxyerythronolide-B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme."
    Bevitt D.J., Cortes J., Haydock S.F., Leadlay P.F.
    Eur. J. Biochem. 204:39-49(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11635 / DSM 40517 / IFO 13426 / JCM 4026 / NCIB 8594.
  4. "Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea."
    Caffrey P., Bevitt D.J., Staunton J., Leadlay P.F.
    FEBS Lett. 304:225-228(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: CA340.
  5. "Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel."
    Tsai S.-C., Miercke L.J.W., Krucinski J., Gokhale R., Chen J.C.-H., Foster P.G., Cane D.E., Khosla C., Stroud R.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:14808-14813(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2890-3172.
  6. "Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases."
    Tsai S.-C., Lu H., Cane D.E., Khosla C., Stroud R.M.
    Biochemistry 41:12598-12606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2890-3172.

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: October 1, 2014
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In each ORF of eryA two modules are present each coding for a functional synthase subunit. Thus eryA showing 3 ORFs codes for 6 synthase subunits. It is supposed that each synthase participates in one 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.
Biosynthesis of polyketides; acyltransferase (AT), beta-ketoacyl carrier protein synthase (KS), and acyl carrier protein (ACP) for chain elongation. Beta-ketoreductase (KR), dehydratase (DH), and enoyl reductase (ER) for processing of the beta carbon, and thioesterase (TE) for release and lactonization of the full-length chain.

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

External Data

Dasty 3