ID B2UP78_AKKM8 Unreviewed; 544 AA.
AC B2UP78;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN OrderedLocusNames=Amuc_2039 {ECO:0000313|EMBL:ACD05849.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05849.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00034270};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP001071; ACD05849.1; -; Genomic_DNA.
DR RefSeq; WP_012421063.1; NZ_CP071807.1.
DR AlphaFoldDB; B2UP78; -.
DR STRING; 349741.Amuc_2039; -.
DR PaxDb; 349741-Amuc_2039; -.
DR KEGG; amu:Amuc_2039; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_7_0_0; -.
DR OrthoDB; 9804858at2; -.
DR BioCyc; AMUC349741:G1GBX-2172-MONOMER; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07941; DRE_TIM_LeuA3; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005675; Citramal_synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00977; citramal_synth; 1.
DR PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/HOMOCITRATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 544 AA; 59307 MW; FF3C6D053A27A709 CRC64;
MSTKIFLYDT TLRDGAQSED VNLSATDKVR IARQLDYLGM DYIEGGWPGA NPVETEFFNA
MRGVGLRNAK LAAFGSTHHP SHTPETDPTL TALISSGARV AAVFGKSCPR HVEVALGISR
ERNLEIIGNS ISFLKKNMEE AFFDAEHFFD GFKRDQEYAL AVLRTAWEHG ADCLVLCDTN
GGTMPEEISS IIRTVRERLP HALLGIHAHN DCELAVANSL AAVNSGAIQV QGTVNGIGER
CGNANLCSVI PNLQVKMKGF SCLSGASLTR LKSTAAFVSE VSNLAPFRRQ PFVGNAAFAH
KGGVHVSAIM KEAALYEHID PSLVGNAQRV LMTEQGGRSN ILSLSRTLGF ELEKGDPLLD
VLSAAVKKNA ALGYDYVAAP ASAELLFLRH MPDNALKPYF NILRTVVLTS RHEMDPDMMV
EASLKLDVHG NVEHTAAGGF GPVHALDRAL RRALTRWYPE LEQMHLIDYK VRVLSPTRTN
IPEAEDENGT GSNVRVLIES SDGVATWTTV GVSYNIIEAS LEALADAVTY KLYKTEQARW
RAEC
//
