AKSA_METJA
ID AKSA_METJA Reviewed; 406 AA.
AC Q57926;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Homocitrate synthase AksA;
DE EC=2.3.3.14 {ECO:0000269|PubMed:9665716};
DE AltName: Full=(R)-homo(2)citrate synthase;
DE EC=2.3.3.- {ECO:0000269|PubMed:9665716};
DE AltName: Full=(R)-homo(3)citrate synthase;
DE EC=2.3.3.- {ECO:0000269|PubMed:9665716};
GN Name=aksA; OrderedLocusNames=MJ0503;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-5, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9665716; DOI=10.1021/bi980662p;
RA Howell D.M., Harich K., Xu H., White R.H.;
RT "Alpha-keto acid chain elongation reactions involved in the biosynthesis of
RT coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic
RT Archaea.";
RL Biochemistry 37:10108-10117(1998).
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:0000269|PubMed:9665716}.
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:0000269|PubMed:9665716};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC Evidence={ECO:0000305|PubMed:9665716};
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:0000269|PubMed:9665716};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44925;
CC Evidence={ECO:0000305|PubMed:9665716};
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:0000269|PubMed:9665716};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44929;
CC Evidence={ECO:0000305|PubMed:9665716};
CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis.
CC {ECO:0000269|PubMed:9665716}.
CC -!- MISCELLANEOUS: Has been shown to catalyze the formation of trans-
CC homoaconitate (PubMed:9665716). However, probably physiologically
CC functions as an (R)-homocitrate/(R)-dihomocitrate/(R)-trihomocitrate
CC synthase. {ECO:0000305|PubMed:9665716}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; L77117; AAB98494.1; -; Genomic_DNA.
DR PIR; G64362; G64362.
DR AlphaFoldDB; Q57926; -.
DR SMR; Q57926; -.
DR STRING; 243232.MJ_0503; -.
DR EnsemblBacteria; AAB98494; AAB98494; MJ_0503.
DR KEGG; mja:MJ_0503; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_4_2_2; -.
DR InParanoid; Q57926; -.
DR PhylomeDB; Q57926; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019298; P:coenzyme B biosynthetic process; IDA:MENGO.
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 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="Homocitrate synthase AksA"
FT /id="PRO_0000140410"
FT DOMAIN 32..285
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 406 AA; 45365 MW; F50D71024B188157 CRC64;
MTKVLVMFMD FLFENSWKAV CPYNPKLDLK DIYIYDTTLR DGEQTPGVCF TKEQKLEIAR
KLDELGLKQI EAGFPIVSER EADIVKTIAN EGLNADILAL CRALKKDIDK AIECDVDGII
TFIATSPLHL KYKFNNKSLD EILEMGVEAV EYAKEHGLFV AFSAEDATRT PIEDLIKVHK
AAEEAGADRV HIADTTGCAT PQSMEFICKT LKENLKKAHI GVHCHNDFGF AVINSIYGLI
GGAKAVSTTV NGIGERAGNA ALEELIMALT VLYDVDLGLN LEVLPELCRM VEEYSGIKMP
KNKPIVGELV FAHESGIHVD AVIENPLTYE PFLPEKIGLK RNILLGKHSG CRAVAYKLKL
MGIDYDREML CEIVKKVKEI REEGKFITDE VFKEIVEEVL RKRNKN
