AKSA_METAC
ID AKSA_METAC Reviewed; 405 AA.
AC Q8TKQ6;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=MA_3342;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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; AE010299; AAM06711.1; -; Genomic_DNA.
DR RefSeq; WP_011023272.1; NC_003552.1.
DR AlphaFoldDB; Q8TKQ6; -.
DR SMR; Q8TKQ6; -.
DR STRING; 188937.MA_3342; -.
DR EnsemblBacteria; AAM06711; AAM06711; MA_3342.
DR GeneID; 1475235; -.
DR KEGG; mac:MA_3342; -.
DR HOGENOM; CLU_022158_4_2_2; -.
DR InParanoid; Q8TKQ6; -.
DR OMA; QIEAGFP; -.
DR OrthoDB; 26145at2157; -.
DR PhylomeDB; Q8TKQ6; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019298; P:coenzyme B biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 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..405
FT /note="Homocitrate synthase AksA"
FT /id="PRO_0000140408"
FT DOMAIN 23..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 405 AA; 45021 MW; CCDB598535106970 CRC64;
MSESEQYSRN TLMDFIEYRP LDIEICDVTL RDGEQTPGVV FTKEQKLAVA SELDSMGIEV
IEAGFPVVSA YEKEIVKEIA NQGYDSRICC LSRAVKGDVD AALDCDVDIV SIFIAMSDMH
LKYKYHRTLE DMLGCAKEAI EYATDHGLNV RFAAEDASRT PIDRLKQAFK EVENEYKVQY
VSLADTIGIL NPTTTHYLVS EIFKCVNTSI CIHCHDDLGM ATANTLAAAE AGAKQLHTTV
NGIGERAGNA SLEEMLVALR VQYGIERYDT TKLTALSRMI SEYSNITPSV NKAVVGQNAF
THESGIHVAA ILEEPRTYEL FLPEMVGGKR NLVVGKHTGT KALKGIINSI GFCLEREELC
ALIEKVKVCT DEKRRSISRE QLEKLIAQVR QEQKPSASEK EKFSI
