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Database: UniProt
Entry: V5EZ15_KALBG
LinkDB: V5EZ15_KALBG
Original site: V5EZ15_KALBG 
ID   V5EZ15_KALBG            Unreviewed;       440 AA.
AC   V5EZ15;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN   ORFNames=PSEUBRA_SCAF13g02007 {ECO:0000313|EMBL:EST09093.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09093.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
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; KI545855; EST09093.1; -; Genomic_DNA.
DR   RefSeq; XP_016294082.1; XM_016434663.1.
DR   AlphaFoldDB; V5EZ15; -.
DR   STRING; 1365824.V5EZ15; -.
DR   GeneID; 27417270; -.
DR   eggNOG; KOG2367; Eukaryota.
DR   HOGENOM; CLU_022158_2_2_1; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 2781767at2759; -.
DR   UniPathway; UPA00033; UER00028.
DR   Proteomes; UP000019377; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          64..317
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  48296 MW;  1A4E22F0440A7585 CRC64;
     MCDHNDPTPI QHVNGGAPDT HVAIDTSAPN HNGSNGVAKD NGNVGNVQPF ASRYSDFLSN
     VSNFKIIEST LREGEQFANA FFDTETKIKI AKALDKFGVD CIELTSPAAS EQSRKDCEAI
     CKLGLKTKVI THIRCHMDDA RIAVETGVDG VDVVMGTSKF LREFSHGKDM TYITKTAIEV
     IQFVKSKGIE IRFSTEDSFR SDLVDLLSIY QAVDKVGVNR VGIADTVGVA NPRQVYDLVR
     TLRGVVGCDI ECHFHNDTGC AIANAYTALE AGATHVDTSV LGIGERNGIP SLGGFIARMY
     TADREYVMSK YNLKALREVE NLVAEAVQIQ VPFNNYVTGY CAFTHKAGIH AKAILANPST
     YEIIRPEDFG MSRYVSIGHR LTGWNAVKSR CEQLELTLTE DQVKEVTAKI KKLADVREQT
     MEDVDSILRN YARAIENGTA
//
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