ID A0A101VPQ5_9FIRM Unreviewed; 380 AA.
AC A0A101VPQ5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Homocitrate synthase {ECO:0000256|RuleBase:RU367143};
DE EC=2.3.3.14 {ECO:0000256|RuleBase:RU367143};
GN Name=aksA {ECO:0000313|EMBL:KUO58408.1};
GN ORFNames=APF84_01560 {ECO:0000313|EMBL:KUO58408.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO58408.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO58408.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO58408.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC {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|RuleBase:RU367143};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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:KUO58408.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOEZ01000088; KUO58408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VPQ5; -.
DR STRING; 1734398.APF84_01560; -.
DR Proteomes; UP000053404; Unassembled WGS sequence.
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 9..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 380 AA; 42087 MW; 1419EC9D8C70C398 CRC64;
MTKLKENGLI IVDTTLRDGE QTAGVVFSNQ EKIRIARMLD EVGVQQIEAG IPVMGGDELE
AIKTICKLGL KASIMGWNRP VIKDIEASVA CGCDSVAISI STSDIHIKHK LNTTRGAVLD
MMVKATEYAK ENFDYISVNA EDASRADMNY LVEFATEARK AGASRVRYCD TIGILEPFTT
YERVKTLIER AEVEVEMHTH NDFGMATANA LAGVRAGARF VGVTVNGLGE RAGNAAMEEV
VMALKHIENN DLDFDTKRFV ELSEYVSRAS GRLLPPWKAI VGSNMFAHES GIHADATLKN
PNTYEVFRPE EVGLERQIVI GKHSGTASIK SKFREYGREI TDEQAKEILK HVRALAIDTK
RSLFDKEIIY IYADLYETDS
//
