(data stored in SCRATCH zone)

SWISSPROT: C8W653_DESAS

ID   C8W653_DESAS            Unreviewed;       293 AA.
AC   C8W653;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU364094};
DE            Short=BCAT {ECO:0000256|RuleBase:RU364094};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU364094};
GN   Name=ilvE {ECO:0000256|RuleBase:RU364094};
GN   OrderedLocusNames=Dtox_0588 {ECO:0000313|EMBL:ACV61508.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61508.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61508.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC       {ECO:0000256|RuleBase:RU364094}.
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:RU364094};
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:RU364094};
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:RU364094};
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:RU364094}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 4/4.
CC       {ECO:0000256|RuleBase:RU364094}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 4/4. {ECO:0000256|RuleBase:RU364094}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004106}.
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DR   EMBL; CP001720; ACV61508.1; -; Genomic_DNA.
DR   RefSeq; WP_015756227.1; NC_013216.1.
DR   STRING; 485916.Dtox_0588; -.
DR   EnsemblBacteria; ACV61508; ACV61508; Dtox_0588.
DR   KEGG; dae:Dtox_0588; -.
DR   eggNOG; ENOG4105CM2; Bacteria.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276706; -.
DR   KO; K00826; -.
DR   OMA; WRGSEMM; -.
DR   OrthoDB; 1275805at2; -.
DR   BioCyc; DACE485916:G1GFV-595-MONOMER; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000002217; 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   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005785; B_amino_transI.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01122; ilvE_I; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W653.
DR   SWISS-2DPAGE; C8W653.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW   Aminotransferase {ECO:0000256|RuleBase:RU364094,
KW   ECO:0000313|EMBL:ACV61508.1};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU364094};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|RuleBase:RU364094,
KW   ECO:0000313|EMBL:ACV61508.1}.
SQ   SEQUENCE   293 AA;  32456 MW;  7751404DE5C7FA0A CRC64;
     MGLIIYLNGN YVPEEQAVVS VFDHGLLYGD GVFEGIRAYH NRVFKLEEHI KRLYESAKTI
     MLDIPLSMEK MSEVVLETLR RNNQRDAYIR LVVTRGKGDL GLDPRKCTKA TVFCITASIQ
     LYPEELYNNG LITVTVPTRR NAGEAVNPRV KSLNYLNNIF AKIEANLAGV PEAVMLNNEG
     YVAEATGDNI FIIKDGVLIT PPVYAGLLEG ITRNCVIEIA RTKGIPVVET LFTRHDIFIA
     DECFLTGTAA ECIPVVQVDG RSIGNGKPGP MTHSLMKAFH ELTETDGPQI FPE
//

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