UniProt: A0A093FR51

Database: UniProt
Entry: A0A093FR51_GAVST

LinkDB:  A0A093FR51_GAVST 
Original site:  A0A093FR51_GAVST

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (17)   
   Pfam (6)   
   PROSITE (2)   
   SMART (4)   
All databases (36)   

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ID   A0A093FR51_GAVST        Unreviewed;      1690 AA.
AC   A0A093FR51;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Fatty acid synthase {ECO:0000256|ARBA:ARBA00018769};
DE            EC=2.3.1.85 {ECO:0000256|ARBA:ARBA00012873};
DE   Flags: Fragment;
GN   ORFNames=N328_09751 {ECO:0000313|EMBL:KFV56794.1};
OS   Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX   NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV56794.1, ECO:0000313|Proteomes:UP000054313};
RN   [1] {ECO:0000313|EMBL:KFV56794.1, ECO:0000313|Proteomes:UP000054313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV56794.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
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DR   EMBL; KK633036; KFV56794.1; -; Genomic_DNA.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000054313; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR049391; FAS_pseudo-KR.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054313}.
FT   DOMAIN          1..401
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   NON_TER         1690
FT                   /evidence="ECO:0000313|EMBL:KFV56794.1"
SQ   SEQUENCE   1690 AA;  184193 MW;  1B8B69B95D800889 CRC64;
     MEDVVIAGIA GKLPESENLQ EFWDNLLNGV DMVTEDDRRW KPGIYGLPKR NGKLKDISKF
     DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPATL RGTDTGVWIG ASGSEAAEAF
     SRDPEELLGY SMTGCQRAML ANRLSYFYNL TGPSMTIDTA CSSSLIALEN AYKAIRHGQC
     SAALVGGVNL LLKPNTSVQF MKLGLLSPDG ACKVFDASGN GYCRSEAVVV VLLMKRSMAK
     RIYATIVNAG SNTDGFKEQG VTFPSGEMQQ QLVSFLCREC GIKPQEVEYI EAHGTGTKVG
     DPQEVNGIVQ VLCQCEREPL LIGSSKSNMG HPEPASGLAA LAKVTDGLRK KIGGGGERNN
     IPGLQDGSLE VVCKPTPVKG GLVSINSFGF GGANAHVILR PNKNKRQPLE TCNTPRLVQI
     CGRTQEAVEI LIEESRKHGG CSPFVSLLND IAAVPVSSMP YRGYTLVGTE SDIKEVQQVQ
     ASGRPLWYIC SGMGTQWKGM GLSLMKLDLF RQSILRSDEA LKNTGLKVSD LLVQADENTF
     DDTVHAFVGL AAIQIAQIDV LKAAGLQPDG ILGHSVGELA CGYADNSLSH EEAILAAYWR
     GRCVKEAKLA PGGMAAVGLT WEECKQRCPP NVVPACHNSE DTVTVSGPLD SVNEFVAKLK
     KDGVFAKEVR SAGVAFHSYY MASIAPVLLS ALKKVIPHPK PRSARWISTS IPESQWQSDL
     ARNSSAEYHV NNLVNPVLFH EGLKHIPENA VVVEIAPHAL LQAILRRALK PTCTVLPLMK
     KEHKNNLEFF LTQTGKIHLT GINVLGNNLF PRVEYPVPVG TPLISPHIKW DHSQDWDVPK
     AADFPAGSKG SASASVYNID VSPDSPDHYL VDHCIDGRVL YPATGYLVLA WRTLARSLDI
     AMEQMAVMFE EVTIHQATIL PKKGSVQLEV RLMPASHCFE VSGNGNLAVS GKISLLENTA
     LKNFHNQPVD FQTQVDMSSK SGLLKEDIYQ ELHLRGYNYG PAFQGVLECN SEASTGKVLW
     NGNWVTFLDA LLHMIILPET GRSLRLPTRI RSVCIDPVLH QEQVCQYQDN VQAFDTVVDR
     CLDSLKAGGV QISGLHASVA PRRQQERIPP TLEKFCFVPY TESNCLSSSV HLHAYLEHCK
     DLIQNLKAKV AVHGVKLVIP GLETAVAAAE SSPIQKGLQH ILAEICRLEL NGNLHSELEQ
     IVTQEKMHLQ IDPLLNGLLD SSELKTCLGV ALENIVSHRI KIVEALAGNG HMFSRVKSIL
     NTQPLLQVDY IATDRILETL SANETELQDA GVSFSQWDPS SLPSGNLTNA DLVVYNCSTN
     VLGNTSEILS NLAAAVKEGG FVLLHTLLKG ETLGEIISFL TSPDLQQKHS FLSEAQWEGL
     FSKASLNLVA LKKSFFGSVI FLCRRQAPAK TPIFLPIDET HYKWVESLKE ILAGPSEQTV
     WLTATSCGNS GILGMVNCLR LEAEGHRIRC VFVSNLNPSS AVPPTSLSSL EMQNIVQRDL
     VMNVYRDGKW GSFRHLPLQQ AQPQELTEYA YVNVLTRGDL SSLRWIVSPL RHFHATNPNV
     QLCKVYYASL NFRDIMLATG KLSPDAIPGN WASQQCMLGM EFAGRDLAGR RVMGLLPAKG
     LATVVDCDKK FLWEVPKNWT LEEAASVPVV YATAFYALVV RGGIKKGESI LIHSGSGGVG
     QAAIAIALSM
//

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