(data stored in SCRATCH zone)

SWISSPROT: D1CDV6_THET1

ID   D1CDV6_THET1            Unreviewed;       393 AA.
AC   D1CDV6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|SAAS:SAAS00085331};
DE            EC=2.3.3.13 {ECO:0000256|SAAS:SAAS00085331};
GN   OrderedLocusNames=Tter_0190 {ECO:0000313|EMBL:ACZ41112.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41112.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41112.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of
CC       acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form
CC       3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
CC       {ECO:0000256|SAAS:SAAS00570112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524,
CC         ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC         EC=2.3.3.13; Evidence={ECO:0000256|SAAS:SAAS01124331};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000256|SAAS:SAAS00085321}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523,
CC       ECO:0000256|SAAS:SAAS00580399}.
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DR   EMBL; CP001825; ACZ41112.1; -; Genomic_DNA.
DR   RefSeq; WP_012874147.1; NC_013525.1.
DR   STRING; 525904.Tter_0190; -.
DR   EnsemblBacteria; ACZ41112; ACZ41112; Tter_0190.
DR   KEGG; ttr:Tter_0190; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046861; -.
DR   KO; K01649; -.
DR   OMA; NDTGMAI; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; TTER525904:G1GGS-193-MONOMER; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005671; LeuA_bact_synth.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR00973; leuA_bact; 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;
DR   PRODOM; D1CDV6.
DR   SWISS-2DPAGE; D1CDV6.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00459460};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|SAAS:SAAS00459450};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Leucine biosynthesis {ECO:0000256|SAAS:SAAS00459347};
KW   Pyruvate {ECO:0000313|EMBL:ACZ41112.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000256|RuleBase:RU003523,
KW   ECO:0000256|SAAS:SAAS00131367, ECO:0000313|EMBL:ACZ41112.1}.
FT   DOMAIN        5    268       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   393 AA;  42934 MW;  0A2BF68D66A673EB CRC64;
     MSEIVRIFDT TLRDGEQSPG VNLSAHEKVL IAEQLVRLGV DIIEAGFPIS SPGDLEAVRQ
     VANTVKGVVV AALARANKAD IDAAWEAVKG AEQPMIHTFI STSDLHIHYK LRKTRDEVLE
     AAEQAVRYAK QFTEEVEFSA EDASRTDPDY LCKVYEVAIN AGATVINVPD TVGYAEPNEF
     SALIRTLYER VPNIHKAVVS VHCHDDLGLA TANTLAAIRE GVGQVEVTIN GIGERAGNTS
     LEEVVMALAT KPAAFNNRKT RINTRELVPT SKLVSQLTGM VVQPNKAIVG ANAFAHEAGI
     HQDGVLKNPL TYEIMTPESV GWQNSKIVLG KHSGRHGFAS RLSEMGIQLS PEELDIAYNQ
     FKRLTDERKH ITDDDLVNLI KSVRASRQEV SIT
//

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