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Database: UniProt
Entry: A0A0A2T5T7_9GAMM
LinkDB: A0A0A2T5T7_9GAMM
Original site: A0A0A2T5T7_9GAMM 
ID   A0A0A2T5T7_9GAMM        Unreviewed;       293 AA.
AC   A0A0A2T5T7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Homocitrate synthase {ECO:0000256|ARBA:ARBA00020735};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN   ORFNames=EP47_13050 {ECO:0000313|EMBL:KGP62793.1};
OS   Legionella norrlandica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1498499 {ECO:0000313|EMBL:KGP62793.1, ECO:0000313|Proteomes:UP000054422};
RN   [1] {ECO:0000313|EMBL:KGP62793.1, ECO:0000313|Proteomes:UP000054422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LEGN {ECO:0000313|EMBL:KGP62793.1,
RC   ECO:0000313|Proteomes:UP000054422};
RA   Rizzardi K., Winiecka-Krusnell J., Ramliden M., Alm E., Andersson S.,
RA   Byfors S.;
RL   Submitted (MAY-2014) 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:KGP62793.1}.
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DR   EMBL; JNCF01000040; KGP62793.1; -; Genomic_DNA.
DR   RefSeq; WP_035890584.1; NZ_JNCF01000040.1.
DR   AlphaFoldDB; A0A0A2T5T7; -.
DR   STRING; 1498499.EP47_13050; -.
DR   OrthoDB; 9803573at2; -.
DR   Proteomes; UP000054422; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..253
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   293 AA;  32923 MW;  5E1EFFA649296D06 CRC64;
     MNPISILDAS LRDGGHRTNF YFKDDDLKKI LVPLDNSGIE YIEIGYRNGS LHPIENIGRA
     GVCQKDYLLY CNSLIKKAKI AVMVHPKNIV EEDLEELKAC GVQLIRICLA RDDLVNAVPI
     LKLAKNLNLE TSVNIIHVSY YSEKELDTLI EEISQYEPNM IYFADSNGSL FPDKINKLYK
     KYTYKYKIPF GFHAHDNLGL AQANALAAIN SGVHFIDASL AGMGKGTGNL KTEFFIAYLH
     ANKIKKYNLE DILTAANYVR DALKIGHEPI EMSEFIRGIS DLSTADLQIF QSN
//
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