ID A0A1N7M4Y0_9RHOB Unreviewed; 538 AA.
AC A0A1N7M4Y0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN05421774_102420 {ECO:0000313|EMBL:SIS81144.1};
OS Gemmobacter megaterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIS81144.1, ECO:0000313|Proteomes:UP000186141};
RN [1] {ECO:0000313|EMBL:SIS81144.1, ECO:0000313|Proteomes:UP000186141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26375 {ECO:0000313|EMBL:SIS81144.1,
RC ECO:0000313|Proteomes:UP000186141};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; FTOT01000002; SIS81144.1; -; Genomic_DNA.
DR RefSeq; WP_076529601.1; NZ_FTOT01000002.1.
DR AlphaFoldDB; A0A1N7M4Y0; -.
DR STRING; 1086013.SAMN05421774_102420; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000186141; Unassembled WGS sequence.
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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Reference proteome {ECO:0000313|Proteomes:UP000186141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 538 AA; 57936 MW; C8BC2241C5B366F8 CRC64;
MRERLYLYDT TLRDGQQTQG VQFSVADKIQ IAQALDLLGV DYIEGGWPGA NPTDSDFFAA
RPQTRATFTA FGMTKRAGRS AANDDVLAAV MNAGTPAVCL VGKTHDFHVT TALGVTLEEN
VEAIGASVAH MVAQGREALF DAEHFFDGFK ANPTYALACL EAAYQAGARW IVLCDTNGGT
LPAEVGRIVA EVVARIPGDR LGIHCHDDTG NAVACSLAAV DAGVRQVQGT LNGLGERCGN
ANLTSLIPTL LLKEPYASRF DTGVARDSLP QMVRISRMLD DILNRVPMRS APYVGASAFA
HKAGLHASAI LKDPSTYEHI EPATVGNTRI IPMSNQAGQS NLRARLAEAG LEVPPGDPRL
ARILDRVKER EDQGFAYDGA QASFEMLARG ELGLVPRFFE IERYRVTVER RRNREGRTVS
LSEAVVVVRI GSQRVLSVSE SLDESGEDRG PVNALSTALA KDLGPYQASI DDMKLVDFKV
RITQGGIDAV TRVMIDSEDG QGRRWSTVGV SPNLVDASFM ALLDAINWKL IRDGVGPA
//