UniProt: C5DMJ8

Database: UniProt
Entry: C5DMJ8_LACTC

LinkDB:  C5DMJ8_LACTC 
Original site:  C5DMJ8_LACTC

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Ontology (7)   
   GO (7)   
Chemical reaction (3)   
   KEGG ENZYME (3)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (31)   

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ID   C5DMJ8_LACTC            Unreviewed;      1738 AA.
AC   C5DMJ8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Fatty acid synthase subunit alpha {ECO:0000256|PIRNR:PIRNR000454};
DE            EC=2.3.1.86 {ECO:0000256|PIRNR:PIRNR000454};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000256|PIRNR:PIRNR000454};
DE              EC=1.1.1.100 {ECO:0000256|PIRNR:PIRNR000454};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000256|PIRNR:PIRNR000454};
DE              EC=2.3.1.41 {ECO:0000256|PIRNR:PIRNR000454};
GN   OrderedLocusNames=KLTH0G09526g {ECO:0000313|EMBL:CAR25009.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR25009.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR25009.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000454};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00001402,
CC         ECO:0000256|PIRNR:PIRNR000454};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC         fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC         Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:83139; EC=2.3.1.86;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000454};
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC       synthetase subunit alpha family. {ECO:0000256|ARBA:ARBA00007485,
CC       ECO:0000256|PIRNR:PIRNR000454}.
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DR   EMBL; CU928171; CAR25009.1; -; Genomic_DNA.
DR   RefSeq; XP_002555446.1; XM_002555400.1.
DR   STRING; 559295.C5DMJ8; -.
DR   GeneID; 8293724; -.
DR   KEGG; lth:KLTH0G09526g; -.
DR   eggNOG; ENOG502SMKZ; Eukaryota.
DR   HOGENOM; CLU_000114_0_0_1; -.
DR   InParanoid; C5DMJ8; -.
DR   OMA; QPILANM; -.
DR   OrthoDB; 2034203at2759; -.
DR   Proteomes; UP000002036; Chromosome G.
DR   GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR   GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00828; elong_cond_enzymes; 1.
DR   Gene3D; 3.30.70.2490; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.90.25.70; -; 1.
DR   Gene3D; 6.10.140.1410; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR040899; Fas_alpha_ACP.
DR   InterPro; IPR047224; FAS_alpha_su_C.
DR   InterPro; IPR026025; FAS_alpha_yeast.
DR   InterPro; IPR041550; FASI_helical.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR   Pfam; PF18325; Fas_alpha_ACP; 1.
DR   Pfam; PF18314; FAS_I_H; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphopantetheine {ECO:0000256|PIRNR:PIRNR000454,
KW   ECO:0000256|PIRSR:PIRSR000454-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000454}.
FT   DOMAIN          1131..1656
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          121..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          357..384
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        1315
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT   MOD_RES         183
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ   SEQUENCE   1738 AA;  192884 MW;  67A3C0A12CAC2BE2 CRC64;
     MSPENQDELC HVLLTELLAY QFAWPVRWVE TQEVLLNERQ TERYIEIGPQ PILANMAKRT
     LKQNENYENA TTISTRREVF SVAGDMDKIC YRYDPPAQSV EKTDAPEENA QGKINDGTEI
     PRAQEISTSC NSSGATSGRS FSTQPELTTE LVVQSVVANK IAGYSIETLP LSHTLKELCK
     GKSTLQNEIK GDLYKELPGL QDAQLEDMSL ESICKEVESP KTLGPVTLGE VTKFIPRKFA
     GKLGTVSAVK EYLSRSWGVN NSAPLLLFIA SRDLKTRFSS EEETQQFIDN SCVEFAKFKK
     IDYSLESAKT NDVGAGCSAE TDEKPKTVDI EVYNECNSDL MQLQKEQHNV MGQHLKVTDA
     QCEIEILKSK LEAMEGKLSA IGEEFGLDYI EKSLTRSFSP LKIRVYDSAW NWGKQSVLQL
     LHAALLNPQK AVEILSPNEI HNLVNRADLS IIKIIQHKLE TEPFSLSVKR RFEGIIQACL
     RDISSQPVYS ATQFTSYEPL GSEHATMQHV RSYDPSQYIK EMSVGTTKSS AETSIVSTKL
     DSDMSSYYKI EKELFQVYSK IIQYSLASNN SPHNIRAQFE TIYEQLLIFL RNSDHVASFF
     RGIINEAVFS VNKSLITTKD DEQDIIVSDC EISSSDDEDD VPPQPVRQTH QPNVSIPTGV
     VPFLHLKRRS HVSGEWIYDK ALTQMYLNNL LRIGKAGVSF SDKRALILVS DAKDNLSLEV
     INALLQAGTV VVVATQRYDH ETTSAFQKSY QKYGASGSKL IVLPLNISSK IDVFRFSEYL
     FSNIGDIDFL LPMNVKATPG SILDYSSEAE LTHRSSSVNL LRLLGCFVKE KRVHAMETRP
     THVLLPLSPN HANIYEESNF KDTFLALVLQ KWYDEDWSTE LSICGCVYGW TNDDGGDLVA
     RGLEKMGVRT FANNEMALNM LGLLSYNVVE CSQESPLIAD LNGGLQTLPN ISSVVSKLQK
     EMATSVEIRE EIEEQARITR ELRGVKEPEV QFVEPKGNVR SDFPQMLPYH EVRAKFNGEQ
     LSGLLDLSQV VVVTGFAEIG PWGSARTRWE MEKSGEFSLE GCIELACVMG LIEYQSSAER
     SGWVDCKSGL PVEEVDIKQR YEAQILEHTG IRIIEPELFQ GYDPKRKQLL HEVIITHDLS
     PIQMDAASAQ QYKLQHGELV EVYPIAETGN SECHVKFLKG CSLMIPKALR LDRFVAGQVP
     TGWDPARYGI GEDITSQVDQ VTLYALIATA EALISSGITD PYEMYQYVHV SEVGNCSGSG
     IGGMNSLRAM RQERLKDTDV QNDIIQETFV NASAAWVNML LLSSSGPIKT PVGACATALE
     SLDNAVETIR SGQAKVCIAG GYDDLEGHVS HEFGNMGATV NSDKELQSGR DPREMCRPAT
     STRAGFLEAH GAGIQVLMSA EVAIEMGVPI YGIVAMTSTA SDKIGRSLPA PGKGILTCAR
     QQPRARSARS AKLDARYRKR QLQARLREID DWAQNELAAG APDVGPAEAR LVQQLAHRQA
     ADAKKHWGNY FWHDNPRVSP LQGALATFGL TVDDLTVASC HGTSTKANEL NESQILDTIM
     QHLGRTPGNP LLAVFQKHLT GHPKGAAGAW MANGLLQLMQ DRVVPGNRNA DNIDQGFRRF
     EHLLYPSENI LVADVKAACL TSFGFGQKGA MAVLVNANYV LAALSESEYT HYAARVRARE
     ARAQRRLADA LVHHTTCRFK DQAPFSAAHE EAVYLDPFAR ADDELRVRPL RDQARGPA
//

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