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Q03133

- ERYA3_SACER

UniProt

Q03133 - ERYA3_SACER

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
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    MSGDNGMTEE KLRRYLKRTV TELDSVTARL REVEHRAGEP IAIVGMACRF     50
    PGDVDSPESF WEFVSGGGDA IAEAPADRGW EPDPDARLGG MLAAAGDFDA 100
    GFFGISPREA LAMDPQQRIM LEISWEALER AGHDPVSLRG SATGVFTGVG 150
    TVDYGPRPDE APDEVLGYVG TGTASSVASG RVAYCLGLEG PAMTVDTACS 200
    SGLTALHLAM ESLRRDECGL ALAGGVTVMS SPGAFTEFRS QGGLAADGRC 250
    KPFSKAADGF GLAEGAGVLV LQRLSAARRE GRPVLAVLAG SAVNQDGASN 300
    GLTAPSGPAQ QRVIRRALEN AGVRAGDVDY VEAHGTGTRL GDPIEVHALL 350
    STYGAERDPD DPLWIGSVKS NIGHTQAAAG VAGVMKAVLA LRHGEMPRTL 400
    HFDEPSPQIE WDLGAVSVVS QARSWPAGER PRRAGVSSFG ISGTNAHVIV 450
    EEAPEADEPE PAPDSGPVPL VLSGRDEQAM RAQAGRLADH LAPEPRNSLR 500
    DTGFTLATRA SAMEHRAVVV GDRDEALAGL RAVADRRIAD RTATGQGPNS 550
    PRRVAMVFPG QGAQWQGMAR DLLRESQVFA DSIRDCERAL APHVDWSLTD 600
    LLSGARPLDR VDVVQPALFA VMVSLAALWR SHGVEPAAVV GHSQGEIAAA 650
    HVAGALTLED AAKLVAVRSR VLRRLGGQGG MASFGLGTEQ AAERIGRFAG 700
    ALSIASVNGP RSVVVVAGES GPLDELIAEC EAEAHKARRI PVDYASHSPQ 750
    VESLREELLT ELAGISPVSA DVALYSTTTG QPIDTATMDT AYWYANLREQ 800
    VRFQDATRQL AEAGFDAFVE VSPHPVLTVG IEATLDSALP ADAGACVVGT 850
    LRRDRGGLAD FHTALGEAYA QGVEVDWSPA FADARPVELP VYPFQRYWLP 900
    IPTGGRARDE DDDWRYQVVW REAEWESASL AGRVLLVTGP GVPSELSDAI 950
    RSGLEQSGAT VLTCDVESRS TIGTALEAAD TDALSTVGVA AVPHGEAVDP 1000
    SLDALALVQA LGAAGVEAPL WVLTRNAVQV ADGELVDPAQ AMVGGLGRVV 1050
    GIEQPGRWGG LVDLVDADAA SIRSLAAVLA DPRGEEQVAI RADGIKVARL 1100
    VPAPARARTH PLEPLAGTVL VTGGTGGIGA HLARWLARSG AEHLVLLGRR 1150
    GADAPGASEL REELTALGTG VTIAACDVAD RARLEAVLAA EAAAEGRTVS 1200
    AVMHAAGVST STPLDDLTEA EFTEIADVKV RGTVNLDELC PDLDAFVLFS 1250
    SNAGVWGSPG LASYAAANAF LDGFARAARS EGAPVTSIAW GLWAGQNMAG 1300
    DEGGEYLRSQ GLRAMDPDRA VEELHITLDH GQTSVSVVDM DRRRFVELFT 1350
    AARHRPLFDE IAGARAEARQ SEEGPALAQR LAALLCDGRE REHLAHLIRA 1400
    EVAAVLGHGD DAAIDRDRAF RDLGFDSMTA VDLRNRLAAV TGVREAATVV 1450
    FDHPTITRLA DHYLERLVGA AEAEQAPALV REVPPKDADD PIAIVGMACR 1500
    FPGGVHNPGE LWEFIVGGGD AVTEMPTDRG WDLDALFDPD PQRHGTSYSR 1550
    HGAFLDGAAD FDAAFFGISP REALAMDPQQ RQVLETTWEL FENAGIDPHS 1600
    VRGSDTGVFL GAAYQGYGQD AVVPEDSEGY LLTGNSSAVV SGRVAYVLGL 1650
    EGPAVTVDTA CSSSLVALHS ACGSLRDGDC GLAVAGGVSV MAGPEVFTEF 1700
    SRQGGLAVDG RCKAFSAEAD GFGLPEGVAV VQLQRLSDGP AEGGRQVLGV 1750
    VAGSAINQDG ATNGLAAPSG VAQQRVIRKA WARAGITGAD VAVVEAHGTG 1800
    TRLGDPVEAS ALLATYGKSR GSSGPVLLGS VKSNIGHAQA AAGVAGVIKV 1850
    VLGLNRGLVP PMLCRGERSP LIEWSSGGVE LAEAVSPWPP AADGVRRAGV 1900
    SAFGVSGTNA HVIIAEPPEP EPLPEPGPVG VLAAANSVPV LLSARTETAL 1950
    AAQARLLESA VDDSVPLTAL ASALATGRAH LPRRAALLAG DHEQLRGQLR 2000
    AVAEGVAAPG ATTGTASAGG VVFVFPGQGA QWEGMARGLL SVPVFAESIA 2050
    ECDAVLSEVA GFSASEVLEQ RPDAPSLERV DVVQPVLFSV MVSLARLWGA 2100
    CGVSPSAVIG HSQGEIAAAV VAGVLSLEDG VRVVALRAKA LRALAGKGGM 2150
    VSLAAPGERA RALIAPWEDR ISVAAVNSPS SVVVSGDPEA LAELVARCED 2200
    EGVRAKTLPV DYASHSRHVE EIRETILADL DGISARRAAI PLYSTLHGER 2250
    RDMGPRYWYD NLRSQVRFDE AVSAQSPDGH ATFVEMSPHP VLTAAVQEIA 2300
    ADAVAIGSLH RDTAEEHLIA ELARAHVHGV AVDWRNVFPA APPVALPNYP 2350
    FEPQRYWLAP EVSDQLADSR YRVDWRPLAT TPVDLEGGFL VHGSAPESLT 2400
    SAVEKAGGVV PVASADREAL AAALREVPGE VAGVLSVHTG AANALALHQS 2450
    LGEAGVRAPL WLVTSRAVAL GESEPVDPEQ AMVWGLGRVM GLETPERWGG 2500
    LVDLPAEPAP GDGEAFVACL GADGHEDQVA IRDHARYGRR LVRAPLGTRE 2550
    SSWEPAGTAL VTGGTGALGG HVARHLARCG VEDLVLVSRR GVDAPAAAEL 2600
    EAELVALGPK TTITACDVAD REQLSKLLEE LRGQGRPVRT VVHTAGVPES 2650
    RPLHEIGELE SVCAAKVTGA RLLDELCPDA ETFVLFSSGA GVWGSANLGA 2700
    YSAANAYLDA LAHRRRAEGR AATSVAWGAW AGEGMATGDL EGLTRRGLRP 2750
    MAPDRAIRAL HQALDNGDTC VSIADVDWEA FAVGFTAARP RPLLDELVTP 2800
    AVGAVPAVQA APAREMTSQE LLEFTHSHVA AILGHSSPDA VGQDQPFTEL 2850
    GFDSLTAVGL RNQLQQATGL ALPATLVFEH PTVRRLADHI GQQLDSGTPA 2900
    REASSALRDG YRQAGVSGRV RSYLDLLAGL SDFREHFDGS DGFSLDLVDM 2950
    ADGPGEVTVI CCAGTAAISG PHEFTRLAGA LRGIAPVRAV PQPGYEEGEP 3000
    LPSSMAAVAA VQADAVIRTQ GDKPFVVAGH SAGALMAYAL ATELLDRGHP 3050
    PRGVVLIDVY PPGHQDAMNA WLEELTATLF DRETVRMDDT RLTALGAYDR 3100
    LTGQWRPRET GLPTLLVSAG EPMGPWPDDS WKPTWPFEHD TVAVPGDHFT 3150
    MVQEHADAIA RHIDAWLGGG NS 3172
    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