ID   A6TTX4_ALKMQ            Unreviewed;       379 AA.
AC   A6TTX4;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Homocitrate synthase {ECO:0000256|RuleBase:RU367143};
DE            EC=2.3.3.14 {ECO:0000256|RuleBase:RU367143};
GN   OrderedLocusNames=Amet_3515 {ECO:0000313|EMBL:ABR49642.1};
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49642.1, ECO:0000313|Proteomes:UP000001572};
RN   [1] {ECO:0000313|Proteomes:UP000001572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX   PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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}.
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DR   EMBL; CP000724; ABR49642.1; -; Genomic_DNA.
DR   RefSeq; WP_012064605.1; NC_009633.1.
DR   AlphaFoldDB; A6TTX4; -.
DR   STRING; 293826.Amet_3515; -.
DR   KEGG; amt:Amet_3515; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_4_2_9; -.
DR   OrthoDB; 9804858at2; -.
DR   Proteomes; UP000001572; 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   Pyruvate {ECO:0000313|EMBL:ABR49642.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          4..255
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   379 AA;  42716 MW;  28C8F0CDAB6453BC CRC64;
     MRDFYIVDTT LRDGEQTPGV VFLKKEKIKI ARMLDELGVD YIEAGIPIMG EEEKDVIREI
     IAMNGKAKIL TWNRMKKMDV DASLACGAKY IHIAVPASDI HIFQKLRKDR KWVIQQVQEV
     VSYGAEKGCI VSVGAEDASR AEEKFLIEIY QAAIKEGAVR LRYADTLGIL TPITTYQAIK
     RICDYIDADL EFHGHNDFGM ATANSLSAFQ AGAKYIDCSV NGLGERAGNT ALEEIVMTLK
     YLLKSNHPFE IKRILELSNI VQEASRKIVG ESKPIVGKSV FSHESGIHVD GLLKNPTVYE
     SFSPGEIGRK RKIVLGKHSG RTTVIYRLQE MGIKVTPKEA NEIIEMIHKK YTYDKNPNID
     HMLQQWVELK RDTYDAFSS
//