ID A0A1I4TA97_9PSEU Unreviewed; 543 AA.
AC A0A1I4TA97;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN05421805_1011353 {ECO:0000313|EMBL:SFM73649.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM73649.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFM73649.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM73649.1,
RC ECO:0000313|Proteomes:UP000199398};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOUP01000001; SFM73649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4TA97; -.
DR STRING; 455193.SAMN05421805_1011353; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000199398; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 15..282
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 543 AA; 57987 MW; 7EF4D70532DAD031 CRC64;
MTRTQPAGTP LGDDFHVYDT TLRDGAQREG ISYSVTDKIA VARLLDSLGV GFVEGGWPGA
LPKDTEFFHR AAQGELELRH AALVAFGSTR RAGAKVDEDP QVRALLESRA PVVTLVAKSD
RRHIERALRT DVAENCAMVA DTVRYLVGEG RRVFLDAEHF FDGYAFDPDT SLRVLESAVQ
AGADVVVLCD TNGGQLPLQL AETVGEVAAR TGFRLGIHCQ DDTGCAVANS IAAVQAGATH
VQCTANGYGE RAGNADLFAV IGNLAAKLGM PVLPEEKLRE LTRTSHALAE IANLAPDTHQ
AYVGQSTFAH KAGLHASAIK VDPELYNHID PAVVGNGMRV LVTEMAGRAS LELKGAELGL
DLSAAPEAVT GAVRRVKELE ARGWSFEAAD ASLELLLRGE MATTTGADPV EAPFELESYR
VVLDHRSDGE VIAEATVKVH VAGERVIATA EGNGPVNALD AALREALVPH LPWLESVELA
DYKVRILTDA RGTDAVTRVL VESRDGEEEW TTVGVHANIV EASWLALCDA LVYKSSRPAF
ATR
//
