AKSA_METMA
ID AKSA_METMA Reviewed; 405 AA.
AC P58967;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=MM_2785;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM32481.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM32481.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048036652.1; NC_003901.1.
DR AlphaFoldDB; P58967; -.
DR SMR; P58967; -.
DR STRING; 192952.MM_2785; -.
DR EnsemblBacteria; AAM32481; AAM32481; MM_2785.
DR GeneID; 44087561; -.
DR GeneID; 66134834; -.
DR KEGG; mma:MM_2785; -.
DR PATRIC; fig|192952.21.peg.3212; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_4_2_2; -.
DR OMA; QIEAGFP; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000000595; 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; 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_0000140414"
FT DOMAIN 23..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 405 AA; 44782 MW; 53F0B002170B4200 CRC64;
MSESEQYSRN TLMDFIDYRP LDIEICDVTL RDGEQTPGVV FSKEQKLAVA SELDSMGIEV
IEAGFPVVSA DEKEIVKEIA NQGFNSRICC LSRAVKGDVD AALECDVDIV SIFIAMSDMH
LKYKYHRSLE DMLGCAKEAI EYATDHGLKV RFAAEDASRT PVERLKQAFK EVENEYKVQY
VSLADTVGIL NPTTTNYLVS EIFKSVNTAI CIHCHDDLGM ATANTLAAAE AGAKQLHTTV
NAIGERAGNA SLEEVLVALR VQYGIERYDT TKLNSLSEMV SEYSGITPSV NKAVVGKNAF
THESGIHVAA ILEEPRTYEL FLPEMVGGKR NLVVGKHTGK KALKGIINSI GFCLEREELC
ALIEKVKVCT EEKHKSISRD QLERLITQVK QEQKPSGSEK EKFSI
