ID H0IZP6_9GAMM Unreviewed; 535 AA.
AC H0IZP6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Homocitrate synthase {ECO:0000256|ARBA:ARBA00020735};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN ORFNames=MOY_04214 {ECO:0000313|EMBL:EHK61848.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK61848.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK61848.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61848.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(2012).
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:EHK61848.1}.
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DR EMBL; AHBC01000015; EHK61848.1; -; Genomic_DNA.
DR AlphaFoldDB; H0IZP6; -.
DR STRING; 1118153.MOY_04214; -.
DR PATRIC; fig|1118153.6.peg.843; -.
DR eggNOG; COG0119; Bacteria.
DR Proteomes; UP000004512; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07944; DRE_TIM_HOA_like; 1.
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:UP000004512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 535 AA; 59687 MW; EB98B4388DF9BD5E CRC64;
MKELKLLDCT LRDGGYYNAW DFSEQLIHEY LDAMQSAGVD IVELGLRTLK KQGFQGPCAF
TTDEFLESLT IPSGLTVGVM VNGSELVGEI PQIEALERLF PNSASNSPVE LVRIACHVHE
FTSSLPAVIW LKDRGYKVGF NLMQVADRTE DEVKALAREA KAYPLDALYF ADSMGSMNPD
QTAKIIQWMR TEWSGPMGIH THDNLGLALS NTLRAIDEGV TWLDSTVTGM GRGPGNARTE
ELAIELAERR DKQVSIVPLM ALLRKHFKPM QEHYGWGTNP YYYLAGKYGI HPTYIQEMLS
DARYDEEDVL AVIEHLRVEG GKKFSLNALD AARHFYRGEA RGNWSPINIF NGRDVLLLGS
GPGVGDHRKA LERYIEKAKP LVVALNTQKC IEAKFVDFRV ACHPVRLLAD CEAHTKLPQP
LITPFSMLPV DVQKSLSEKE ILDYGLKVKA NTFSFDENAC TVPSSLVVAY ALAVLNSGKA
NKIMMAGFDG YGADDPRSQE MHQLFEEYLA NKETVRLVSI TPTRYALHTE SVYAL
//
