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Database: UniProt
Entry: G7J960_MEDTR
LinkDB: G7J960_MEDTR
Original site: G7J960_MEDTR 
ID   G7J960_MEDTR            Unreviewed;       537 AA.
AC   G7J960;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=3-ketoacyl-CoA synthase {ECO:0000256|PIRNR:PIRNR036417};
DE            EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR036417};
GN   Name=11431933 {ECO:0000313|EnsemblPlants:AES73501};
GN   OrderedLocusNames=MTR_3g105550 {ECO:0000313|EMBL:AES73501.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES73501.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES73501.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES73501.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES73501,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES73501.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73501,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES73501}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73501};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC         chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC         EC=2.3.1.199; Evidence={ECO:0000256|ARBA:ARBA00001906};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|PIRNR:PIRNR036417}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000256|ARBA:ARBA00005531,
CC       ECO:0000256|PIRNR:PIRNR036417}.
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DR   EMBL; CM001219; AES73501.1; -; Genomic_DNA.
DR   RefSeq; XP_003603250.1; XM_003603202.2.
DR   AlphaFoldDB; G7J960; -.
DR   STRING; 3880.G7J960; -.
DR   PaxDb; 3880-AES73501; -.
DR   EnsemblPlants; AES73501; AES73501; MTR_3g105550.
DR   GeneID; 11431933; -.
DR   Gramene; AES73501; AES73501; MTR_3g105550.
DR   KEGG; mtr:11431933; -.
DR   eggNOG; ENOG502QU93; Eukaryota.
DR   HOGENOM; CLU_013238_2_0_1; -.
DR   OMA; PENTATM; -.
DR   OrthoDB; 930987at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002051; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00831; CHS_like; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR012392; 3-ktacl-CoA_syn.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR013601; FAE1_typ3_polyketide_synth.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR31561; 3-KETOACYL-COA SYNTHASE; 1.
DR   PANTHER; PTHR31561:SF2; 3-KETOACYL-COA SYNTHASE 10; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   Pfam; PF08392; FAE1_CUT1_RppA; 1.
DR   PIRSF; PIRSF036417; 3-ktacl-CoA_syn; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR036417};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036417};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..404
FT                   /note="FAE"
FT                   /evidence="ECO:0000259|Pfam:PF08392"
FT   DOMAIN          431..511
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        339
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        436
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        465
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036417-1"
SQ   SEQUENCE   537 AA;  60669 MW;  683F113B9065FED9 CRC64;
     MATNEGDMFS AEIVNRGIES SGPNAGSLTF SVRVRRRLPD FLQSVNLKYV KLGYHYLINH
     GVYLFTIPIL LVVFSAEVGS LSKEDLWKKI WEDATYDLAS VLSSLAVFVF TFTLYFMSRP
     RPIYLIDFAC YQPDDELKVS REQLIELARK SGKFDEGSLE FQKRIVMSSG IGDETYIPRS
     VISSSENTAT MKEGRAEASM VMFGALDELF EKTGIRPKDV GVLVVNCSIF NPTPSLSAMI
     INHYKMRGNI LSYNLGGMGC SAGIIAVDLA RDILQSNPGN YAVVVSTEMV GFNWYQGKER
     SMLIPNCFFR MGCSAVLLSN RRRDFGRAKY RLEHIVRTHK GADDRSFRCV YQEEDDQKFK
     GIKISKDLIE IGGEALKTNI TTLGPLVLPF SEQLIFFATL VWRNWFGGGK SDKNSPSSNK
     PYIPNYKLAF EHFCVHAASK TILDELQKNL ELSDKNMEAS RMTLHRFGNT SSSSIWYELA
     YMEAKEKVKR GDRVWQLAFG SGFKCNSAVW RSMRRVTKPS SRNPWLDCID AYPASLN
//
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