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
//