ID A0A160JDM1_9PROT Unreviewed; 373 AA.
AC A0A160JDM1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Homocitrate synthase {ECO:0000256|ARBA:ARBA00020735, ECO:0000256|RuleBase:RU367143};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974, ECO:0000256|RuleBase:RU367143};
GN Name=nifV {ECO:0000313|EMBL:ANC90810.1};
GN ORFNames=A6A40_02225 {ECO:0000313|EMBL:ANC90810.1};
OS Azospirillum humicireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC90810.1, ECO:0000313|Proteomes:UP000077405};
RN [1] {ECO:0000313|EMBL:ANC90810.1, ECO:0000313|Proteomes:UP000077405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC90810.1,
RC ECO:0000313|Proteomes:UP000077405};
RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
CC -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC {ECO:0000256|ARBA:ARBA00003050, ECO:0000256|RuleBase:RU367143}.
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 ECO:0000256|RuleBase:RU367143};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP015285; ANC90810.1; -; Genomic_DNA.
DR RefSeq; WP_063633915.1; NZ_CP015285.1.
DR AlphaFoldDB; A0A160JDM1; -.
DR STRING; 1226968.A6A40_02225; -.
DR KEGG; ahu:A6A40_02225; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000077405; Chromosome.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd07939; DRE_TIM_NifV; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013477; NifV/FrbC.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02660; nifV_homocitr; 1.
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; 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 Nitrogen fixation {ECO:0000256|RuleBase:RU367143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 6..257
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 373 AA; 40086 MW; F2F06595751684D7 CRC64;
MPTTFATIND TTLRDGEQTA GVAFTLDEKI AIAKALDAAG VPEQEVGIPA MGEEEREGIR
AVAALGLKGR LMVWCRMHDA DLKAALSCNV GFVNLSMPVS DIHITRKLKR SRAWALAEIE
RRVKQARDHG LEVSVGGEDS SRADMDFLIA AATVAQQAGA RRFRFADTLG VLDPFQTRAC
IERLRRATDL EIEIHAHDDL GLANANSLAA VLGGATHVNT TVNGLGERAG NAPLEEVVVS
LKHLYHIDTG VETRSLGTIS DLVERASNRP VAVNKSIVGA AVFTHEAGIH VDGLLRDRAT
YQNFDPAEVG REHRIVLGKH SGTAAVKLAY ERLGIACDDA TAQAVLPRVR ALATRAKRPP
TPEELHAFLE AAT
//
