(data stored in SCRATCH zone)

SWISSPROT: Q47SB3_THEFY

ID   Q47SB3_THEFY            Unreviewed;       373 AA.
AC   Q47SB3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   OrderedLocusNames=Tfu_0616 {ECO:0000313|EMBL:AAZ54654.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54654.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-
CC         oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146,
CC         ChEBI:CHEBI:58045; EC=2.6.1.42;
CC         Evidence={ECO:0000256|RuleBase:RU004517};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate +
CC         L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427;
CC         EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU004517};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC         glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762;
CC         EC=2.6.1.42; Evidence={ECO:0000256|RuleBase:RU004517};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004516};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 4/4.
CC       {ECO:0000256|RuleBase:RU004519}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 4/4.
CC       {ECO:0000256|RuleBase:RU004519}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 4/4. {ECO:0000256|RuleBase:RU004519}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004106}.
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DR   EMBL; CP000088; AAZ54654.1; -; Genomic_DNA.
DR   RefSeq; WP_011291063.1; NC_007333.1.
DR   STRING; 269800.Tfu_0616; -.
DR   EnsemblBacteria; AAZ54654; AAZ54654; Tfu_0616.
DR   KEGG; tfu:Tfu_0616; -.
DR   eggNOG; ENOG4105CM2; Bacteria.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276704; -.
DR   KO; K00826; -.
DR   OMA; NFFGITH; -.
DR   OrthoDB; 1275805at2; -.
DR   BioCyc; TFUS269800:G1G4Q-627-MONOMER; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01557; BCAT_beta_family; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR033939; BCAT_family.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SB3.
DR   SWISS-2DPAGE; Q47SB3.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|RuleBase:RU004517,
KW   ECO:0000313|EMBL:AAZ54654.1};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU004517};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU004517,
KW   ECO:0000313|EMBL:AAZ54654.1}.
FT   MOD_RES     208    208       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR006468-1}.
SQ   SEQUENCE   373 AA;  40701 MW;  75272274AFC05706 CRC64;
     MSNGTTTSGL TFDIRLSTER KTPQEREAIL ENPGFGKVFT DHMVTIRYTA DRGWHDARLE
     PYGPLSLDPA TSVLHYAQEI FEGLKAYRHP DGSIACFRPE ANAARFNSSA KRMAMPELPE
     ELFLGAIDTL LTYDGDWVPT QADTSLYLRP FMISTDVGLG VNSPSSSYLF VLIASPSGGY
     FANGVKPVTV WLCEDYTRAA PGGTGAAKFG GNYAASFLAQ AQAVEQGCDQ VVWLDAVEHR
     WVEEMGGMNL FFVFGSGENA RLLTPELTGT LLPGITRDSL LKLAPDLGYP VEEGRISTDE
     WREAAASGEL TEVFACGTAA VITPVSHVKS RQGEFQIGDG TPGPITMRLR EELVGLQYGT
     RPDSHGWIRK FGR
//

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