ID A0A1H2TAC7_9FLAO Unreviewed; 498 AA.
AC A0A1H2TAC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=D-citramalate synthase {ECO:0000313|EMBL:SDW40655.1};
GN ORFNames=SAMN05444411_101656 {ECO:0000313|EMBL:SDW40655.1};
OS Lutibacter oricola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=762486 {ECO:0000313|EMBL:SDW40655.1, ECO:0000313|Proteomes:UP000199595};
RN [1] {ECO:0000313|EMBL:SDW40655.1, ECO:0000313|Proteomes:UP000199595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24956 {ECO:0000313|EMBL:SDW40655.1,
RC ECO:0000313|Proteomes:UP000199595};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; FNNJ01000001; SDW40655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2TAC7; -.
DR STRING; 762486.SAMN05444411_101656; -.
DR Proteomes; UP000199595; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.340; -; 1.
DR Gene3D; 3.30.160.740; -; 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; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF57; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 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:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000199595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 1..261
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 498 AA; 55634 MW; 421CE9AEDF4E17DB CRC64;
MDTTLRDGEQ TSGVSFPSAE KLTIAKLLLE ELNVDRIEVA SARVSEGEFQ AVKAITDWAN
ENGYINRIEM LTFVDGGRSI EWMDKAGAKV QNLLTKGSLN HLTHQLKKTP EQHFAEIKNV
VELAQNAGIK TNVYLEDWSN GMHNSPEYVF QFLDFLETLS LERILLPDTL GVLTHNETFD
YFSKITAKYP NTHFDFHAHN DYDLGVANVM ESIKAGASGL HLTVNGMGER AGNAPMASVI
AVINDFFKDE VEIQVKETSL YSVSKIIETF SGIRIPSNKP IVGDNVFTQT AGIHADGDNK
NNLYFNDLMP ERFGRKRKYA LGKTSGKANI EKNLQELGLE LDQVDLLKVT ERIIELGDKK
ELVTKEDLPY IISDVLDSSL YEERITVESY VLTHSKGLKP STTVAVKIDG DLYEEHAQGD
GQFDAFMNAL RKLYKKKNMT MPSLVDYAVR IPPGSTSAAL CETIITWESD SNKFITRGLD
CDQTVSAIKA TQKMLNIR
//
