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Database: UniProt
Entry: A0A433JL81_9GAMM
LinkDB: A0A433JL81_9GAMM
Original site: A0A433JL81_9GAMM 
ID   A0A433JL81_9GAMM        Unreviewed;       297 AA.
AC   A0A433JL81;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Homocitrate synthase {ECO:0000256|ARBA:ARBA00020735};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN   ORFNames=EKM59_02685 {ECO:0000313|EMBL:RUQ90060.1};
OS   Legionella septentrionalis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=2498109 {ECO:0000313|EMBL:RUQ90060.1, ECO:0000313|Proteomes:UP000288012};
RN   [1] {ECO:0000313|EMBL:RUQ90060.1, ECO:0000313|Proteomes:UP000288012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=km714 {ECO:0000313|Proteomes:UP000288012};
RA   Wu H.;
RT   "Legionella sp,whole genome shotgun sequence.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC       {ECO:0000256|ARBA:ARBA00003050}.
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:ARBA00000596};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUQ90060.1}.
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DR   EMBL; RZGR01000005; RUQ90060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433JL81; -.
DR   Proteomes; UP000288012; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR   PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000288012};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..252
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   297 AA;  32934 MW;  200DC0563CEA0562 CRC64;
     MNIQALDVTL RDGGNRTNFH FSDEDIQHIL SGLDNSGIEY IEIGYRNGSI HPIPDLGRAG
     LCAKNYLAYC TSLIHHSRIA VMAHPQNLTQ ADLEELKSFG ISMIRICIAK GDVQAAYSIM
     QDCRKLGFIT SANFIHISQY HEPELDEAVE QISQISPDIV YFADSNGSLL PAKVKKMYEK
     YVNAYSMAFG FHAHDNLGLA QANAIAAAGA GVSYIDFSLA GMGKGIGNLR TEYFTAYLHA
     LNIKKYRLES ILPAANYVRK MFHTEQENIP MDEFERGILD LSTAEIKTKN STNNKAS
//
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