ID D7J8R9_9BACE Unreviewed; 515 AA.
AC D7J8R9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:EFI12030.1};
GN ORFNames=HMPREF0106_03787 {ECO:0000313|EMBL:EFI12030.1};
OS Bacteroides sp. D22.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=585544 {ECO:0000313|EMBL:EFI12030.1, ECO:0000313|Proteomes:UP000003817};
RN [1] {ECO:0000313|EMBL:EFI12030.1, ECO:0000313|Proteomes:UP000003817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D22 {ECO:0000313|EMBL:EFI12030.1,
RC ECO:0000313|Proteomes:UP000003817};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Sibley C., White A., Ambrose C.E., Allen-Vercoe E.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain D22.";
RL Submitted (MAR-2010) 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; GG774817; EFI12030.1; -; Genomic_DNA.
DR RefSeq; WP_004315473.1; NZ_GG774817.1.
DR AlphaFoldDB; D7J8R9; -.
DR GeneID; 61623928; -.
DR HOGENOM; CLU_022158_0_1_10; -.
DR Proteomes; UP000003817; 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 CDD; cd07945; DRE_TIM_CMS; 1.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 8..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 515 AA; 57786 MW; CDBF471A09F3BA53 CRC64;
MGKEGVKIEI MDTTLRDGEQ TSGVSFVPHE KLMIARLLLE DLKVDRVEVA SARVSDGEFE
AVKMICDWAA RRNLLHKVEV LGFVDGHTSV DWIQRTGCRV INLLCKGSLK HCTQQLKKTP
EEHLADIINV VHYADEQDIT VNVYLEDWSN GIKDSPEYVF QLMDGLQETS VKRYMLPDTL
GILNPLQVIE YMRKMKKRYP NTHLDFHAHN DYDLAVSNVL AAVLSGVKGL HTTINGLGER
AGNAPLASVQ AILKDHFNAA TNIDESRLND VSRVVESYSG IMIPANKPIV GENVFTQVAG
VHADGDNKNN LYCNDLLPER FGRKREYALG KTSGKANIRK NLEDLGLELD EDAMRKVTER
IIELGDKKEL VTQEDLPYIV SDVLKHGAIG EKVKLKSYFV NLAHGLKPMA TLKIEINGKE
YEESSGGDGQ YDAFVRALRK IYKVTLGRKF PMLTNYAVTI PPGGRTDAFV QTVITWSYDE
QVFRTRGLDA DQTEAAIKAT MKMLNLIEDE YEKSK
//
