(data stored in ACNUC7421 zone)

SWISSPROT: Q5LX36_RUEPO

ID   Q5LX36_RUEPO            Unreviewed;       288 AA.
AC   Q5LX36;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
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   ECO:0000313|EMBL:AAV93573.1};
GN   OrderedLocusNames=SPO0253 {ECO:0000313|EMBL:AAV93573.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93573.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93573.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93573.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93573.1; -; Genomic_DNA.
DR   RefSeq; WP_011046015.1; NC_003911.12.
DR   STRING; 246200.SPO0253; -.
DR   EnsemblBacteria; AAV93573; AAV93573; SPO0253.
DR   KEGG; sil:SPO0253; -.
DR   eggNOG; ENOG4105CM2; Bacteria.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276706; -.
DR   KO; K00826; -.
DR   OMA; WRGSEMM; -.
DR   OrthoDB; 1275805at2; -.
DR   BioCyc; RPOM246200:G1G48-258-MONOMER; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000001023; 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; Q5LX36.
DR   SWISS-2DPAGE; Q5LX36.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW   Aminotransferase {ECO:0000256|RuleBase:RU364094,
KW   ECO:0000313|EMBL:AAV93573.1};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU364094};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|RuleBase:RU364094,
KW   ECO:0000313|EMBL:AAV93573.1}.
SQ   SEQUENCE   288 AA;  31945 MW;  73646EA21024DD5E CRC64;
     MASYDDRDGV IWMDGELVDW RDAKVHILTH AMHYASSVFE GERAYNGKIF KSREHSERLV
     ASAQALDMPM PYTVDQIEAA KEETLKASGL TDAYVRALVW RGSGEDMGVA SARNPVRMAI
     AVWPWGAYYG DAKMQGAKLD IAEWKRPSPE TIPVHAKAAG LYMICTISKH KAEAKGCSDA
     LFMDWRGYVA EATGANVFFV KDGEVHTPLA DCFLNGITRQ TVIGMLKDKG ITVHERRIKP
     EEMEGFEQCW LTGTAAEVTP VGQIGPYTFE VGQMTRDIAA EYEALVRA
//

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