ID   AKSA_METKA              Reviewed;         397 AA.
AC   Q8TW28;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Homocitrate synthase AksA;
DE            EC=2.3.3.14 {ECO:0000250|UniProtKB:Q57926};
DE   AltName: Full=(R)-homo(2)citrate synthase;
DE            EC=2.3.3.- {ECO:0000250|UniProtKB:Q57926};
DE   AltName: Full=(R)-homo(3)citrate synthase;
DE            EC=2.3.3.- {ECO:0000250|UniProtKB:Q57926};
GN   Name=aksA; OrderedLocusNames=MK1209;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC   -!- FUNCTION: Catalyzes the condensation of alpha-ketoglutarate and acetyl-
CC       CoA to form (R)-homocitrate. Can also catalyze the condensation of
CC       alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the
CC       condensation of alpha-ketopimelate with acetyl-CoA to form (R)-
CC       homo(3)citrate. These reactions are part of the biosynthesis pathway of
CC       coenzyme B and biotin. {ECO:0000250|UniProtKB:Q57926}.
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:0000250|UniProtKB:Q57926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC         Evidence={ECO:0000250|UniProtKB:Q57926};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoadipate + acetyl-CoA + H2O = (R)-dihomocitrate + CoA +
CC         H(+); Xref=Rhea:RHEA:44924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57499,
CC         ChEBI:CHEBI:72697; Evidence={ECO:0000250|UniProtKB:Q57926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44925;
CC         Evidence={ECO:0000250|UniProtKB:Q57926};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoheptanedioate + acetyl-CoA + H2O = (R)-trihomocitrate +
CC         CoA + H(+); Xref=Rhea:RHEA:44928, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:72699, ChEBI:CHEBI:72701;
CC         Evidence={ECO:0000250|UniProtKB:Q57926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44929;
CC         Evidence={ECO:0000250|UniProtKB:Q57926};
CC   -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis.
CC       {ECO:0000250|UniProtKB:Q57926}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AE009439; AAM02422.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TW28; -.
DR   SMR; Q8TW28; -.
DR   STRING; 190192.MK1209; -.
DR   EnsemblBacteria; AAM02422; AAM02422; MK1209.
DR   KEGG; mka:MK1209; -.
DR   PATRIC; fig|190192.8.peg.1311; -.
DR   HOGENOM; CLU_022158_4_2_2; -.
DR   OMA; QIEAGFP; -.
DR   UniPathway; UPA00919; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011830; LEU1_arch.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR02090; LEU1_arch; 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   Reference proteome; Transferase.
FT   CHAIN           1..397
FT                   /note="Homocitrate synthase AksA"
FT                   /id="PRO_0000140412"
FT   DOMAIN          19..270
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   397 AA;  43750 MW;  3D81E012BC8E9DAC CRC64;
     MQSPYVREAV REMDLPDEVI VYDTTLRDGE QTPGVSFTPE QKLEIAHLLD ELGVQQIEAG
     FPVVSEGERD AVRRIAHEGL NADILCLART LRGDVDAALD CDVDGVITFI ATSELHLKHK
     LRMSREEVLE RIADTVEYAK DHGLWVAFSA EDGTRTEFEF LERVYRTAEE CGADRVHATD
     TVGVMIPAAM RLFVAKIREV VDLPIGVHCH DDFGMAVANS LAAVEAGAQA ISTTVNGIGE
     RAGNAALEEV IMALKELYGI DPGFNTEVLA ELSRKVSEYS GIDVPPNKAV VGENAFRHES
     GIHVAAVLEE PRTYEPIDPK EVGMNRKIVL GKHTGRKAVV AKLEELGVEP EEEIVEEVLK
     RIKALGDRRV RVTDSKLEEI VRNVLESRGD RDDPGSR