ID A0A0J9UCC3_FUSO4 Unreviewed; 439 AA.
AC A0A0J9UCC3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN ORFNames=FOXG_01159 {ECO:0000313|EMBL:KNA95705.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNA95705.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNA95705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNA95705.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNA95705.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNA95705.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58884; EC=2.3.3.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC Evidence={ECO:0000256|ARBA:ARBA00000523};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC {ECO:0000256|ARBA:ARBA00004755}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. Homocitrate synthase LYS20/LYS21 subfamily.
CC {ECO:0000256|ARBA:ARBA00006361}.
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DR EMBL; DS231696; KNA95705.1; -; Genomic_DNA.
DR RefSeq; XP_018233751.1; XM_018377949.1.
DR AlphaFoldDB; A0A0J9UCC3; -.
DR GeneID; 28943430; -.
DR KEGG; fox:FOXG_01159; -.
DR VEuPathDB; FungiDB:FOXG_01159; -.
DR OrthoDB; 2781767at2759; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000009097; Unassembled WGS sequence.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR CDD; cd07948; DRE_TIM_HCS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02222; Homocitr_synth_fung_arch; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR048253; DRE_TIM_HCS_fun_bact.
DR InterPro; IPR011872; Homocitrate_synth.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02146; LysS_fung_arch; 1.
DR PANTHER; PTHR10277:SF48; HOMOCITRATE SYNTHASE, CYTOSOLIC ISOZYME-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 40..289
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 47746 MW; 6C7A0B38EE99F748 CRC64;
MCGTENGSVG AAPHPAQNAN NPATSVYSQV QDFLSNTNRY KIIESTLREG EQFSNAFFTR
ENKVKIATML SDFGVDYIEL TSPVSSQASY DDCKHICSLG LKAKILTHVR CNMDDAKRAV
ECGVDGVDLV IGTSSFLREY SHGKSMEMIQ KTAIEVIEYV KSQGVEVRFS SEDSFRSDLV
DILALYKAVD KAGVNRVGIA DTVGGATPRM VYDLVRTLRG KRETHFHDDT GCAVANAVTA
LEGGATHVDT SVLGIGERNG ITPLGALMAR MVVTAPEYTK THYKLPKLKE IEEYVASVVQ
VNIPFNNPIT GFCAFTHKAG IHAKAILANP STYEIIDPAL FGLTRYVNIT SRITGWNAVK
GRISQLGLDG PGGFETDDQI KEVTAKIKQM ADSEQPFPVQ GLSFVRPLAI DDADSIIHAY
HLGLQGQSEQ QNASEQKEA
//
