ID A0A1N6DZ62_9BACT Unreviewed; 507 AA.
AC A0A1N6DZ62;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-citramalate synthase {ECO:0000313|EMBL:SIN75997.1};
GN ORFNames=SAMN04488055_1186 {ECO:0000313|EMBL:SIN75997.1};
OS Chitinophaga niabensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=536979 {ECO:0000313|EMBL:SIN75997.1, ECO:0000313|Proteomes:UP000185003};
RN [1] {ECO:0000313|EMBL:SIN75997.1, ECO:0000313|Proteomes:UP000185003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24787 {ECO:0000313|EMBL:SIN75997.1,
RC ECO:0000313|Proteomes:UP000185003};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FSRA01000001; SIN75997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6DZ62; -.
DR STRING; 536979.SAMN04488055_1186; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000185003; 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:UP000185003};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 8..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 507 AA; 56332 MW; 7C64F27EF500FD31 CRC64;
MPSAQRYIEI MDTTLRDGEQ TSGVSFSPSE KLTIAQLLLT EVKVDRIEIA SARVSEGEFA
AVKSITKWAK ANGLLDRVEV LTFVDGDVSV QWMLKAGAKV MNLLTKGSLN HLTHQLKKKP
EEHFAEVGAV IKLAKKKGLE CNVYLEDWSN GMRHSKDYVF QYLDFLNTQP VKRVMLPDTL
GILTPAEVTS FVSETIQRYP NIHFDFHAHN DYDLGTANVL EGVKAGAHGI HLTINGMGER
AGNAPLASAI AVLNDFMPEL KTGVAEGSLY KVSKLVETFS GFRIPVNKPV VGENVFTQTA
GIHADGDKKN KLYFSDLIPE RFGRTRKYAL GKTSGKANIE NNLQQLGLQL SDPDLKKVTQ
RIIELGDKKE VVTQADLPYI ISDVLDSNTI EEKVTVLDYV LTHSKTLKPS VTLRIAILEE
IFEEHSQGDG QYDAFMNALK KVYKKLKQEL PVLTDYAVRI PPGGKSDALC ETIITWRHSN
KEFKTRGLDS DQTVSAIKAT QKMLNLI
//
