AKSA_METTH
ID AKSA_METTH Reviewed; 391 AA.
AC O27667;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=MTH_1630;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB86103.1; -; Genomic_DNA.
DR PIR; H69084; H69084.
DR RefSeq; WP_010877238.1; NC_000916.1.
DR AlphaFoldDB; O27667; -.
DR SMR; O27667; -.
DR STRING; 187420.MTH_1630; -.
DR PRIDE; O27667; -.
DR EnsemblBacteria; AAB86103; AAB86103; MTH_1630.
DR GeneID; 24854732; -.
DR KEGG; mth:MTH_1630; -.
DR PATRIC; fig|187420.15.peg.1594; -.
DR HOGENOM; CLU_022158_4_2_2; -.
DR OMA; QIEAGFP; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000005223; 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..391
FT /note="Homocitrate synthase AksA"
FT /id="PRO_0000140416"
FT DOMAIN 20..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 391 AA; 43966 MW; A9611698121602FE CRC64;
MRYFVSPFNK EAELKFPDRI TIYDTTLRDG EQTPGVCLGT EEKLEIARKL DELGIHQIES
GFPVVSEQER VSVKSIANEG LNAEILALCR TKKDDIDAAI DCDVDGVITF MATSDLHLKH
KLKLTREEAL NVCMNSIEYA KDHGLFLAFS AEDATRTDLD FLKQIYRKAE NYGADRVHIA
DTVGAISPQG MDYLVRELRR DIKVDIALHC HNDFGMALSN SIAGLLAGGT AVSTTVNGIG
ERAGNTSLEE LIMALRIIYE VDLGFNIGVL YELSRLVEKH TRMKVPENKP IVGRNVFRHE
SGIHVDAVIE EPLTYEPFLP EMIGHQRKIV LGKHSGCRAV KAKLEEYGID VTRDELCRIV
EEVKKNREKG KYINDELFYR IVKSVRGPVD F
