(data stored in ACNUC7421 zone)

SWISSPROT: Q47SB2_THEFY

ID   Q47SB2_THEFY            Unreviewed;       527 AA.
AC   Q47SB2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:AAZ54655.1};
DE            EC=2.3.3.13 {ECO:0000313|EMBL:AAZ54655.1};
GN   OrderedLocusNames=Tfu_0617 {ECO:0000313|EMBL:AAZ54655.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54655.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54655.1; -; Genomic_DNA.
DR   RefSeq; WP_011291064.1; NC_007333.1.
DR   STRING; 269800.Tfu_0617; -.
DR   EnsemblBacteria; AAZ54655; AAZ54655; Tfu_0617.
DR   KEGG; tfu:Tfu_0617; -.
DR   eggNOG; ENOG4105CYQ; Bacteria.
DR   eggNOG; COG0119; LUCA.
DR   HOGENOM; HOG000046860; -.
DR   KO; K01649; -.
DR   OMA; NDTGMAI; -.
DR   OrthoDB; 840579at2; -.
DR   BioCyc; TFUS269800:G1G4Q-628-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 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   PANTHER; PTHR43538; PTHR43538; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR00977; citramal_synth; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SB2.
DR   SWISS-2DPAGE; Q47SB2.
KW   Acyltransferase {ECO:0000313|EMBL:AAZ54655.1};
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00161459};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|SAAS:SAAS00160591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU003523,
KW   ECO:0000256|SAAS:SAAS00131367, ECO:0000313|EMBL:AAZ54655.1}.
FT   DOMAIN        6    272       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   527 AA;  56901 MW;  CE15B8C095DE0912 CRC64;
     MLDDSFHVFD TTLRDGAQRE GINFTVADKL AVAKLLDEFG VGFIEGGWPG ANPKDTEFFR
     RAQTELSLKH AQLTAFGSTR RAGTTAAKDP QVLALRDSGA PVVTLVAKSD DRHVELALRT
     TLEENLEMIA DTVSFLLGQG QRVFVDCEHF FDGYRHNPEY ALRVVRTAAE AGASVVVLCD
     TNGGMLPSDV FQIVSEVREA TGARLGIHAQ DDSGCAVANT LAAVDAGATH VQCTANGYGE
     RVGNANLFSV VPALVLKRGR NVLPEGCLRE MTRVSQAIAE IANIAPATHQ PYVGISAFAH
     KAGLHASAIK VDPDLYQHID PALVGNDMRM LVSDMAGRAS VELKAKELGV DLSGDRETLG
     RIVERVKDME MAGYSFEAAD ASLELLLREE IGQPVRYFEV ESWRTISERR PDGSSASEAT
     VKLYVKGERV VATGEGNGPV NALDRALRSA LESVYPDLAT MELVDYKVRI LEGTSGTDAV
     TRVLIDCSDG QGEWTTVGVG ENVIEASWTA LEQALTYGLL RRGYTQQ
//

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