(data stored in SCRATCH zone)

SWISSPROT: A4AVL1_MARSH

ID   A4AVL1_MARSH            Unreviewed;       279 AA.
AC   A4AVL1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   OrderedLocusNames=FB2170_01167 {ECO:0000313|EMBL:EAQ99941.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99941.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99941.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004106}.
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DR   EMBL; CP002157; EAQ99941.1; -; Genomic_DNA.
DR   STRING; 313603.FB2170_01167; -.
DR   EnsemblBacteria; EAQ99941; EAQ99941; FB2170_01167.
DR   KEGG; fbc:FB2170_01167; -.
DR   eggNOG; ENOG4105CM2; Bacteria.
DR   eggNOG; COG0115; LUCA.
DR   HOGENOM; HOG000276704; -.
DR   KO; K00826; -.
DR   OMA; NFFGITH; -.
DR   Proteomes; UP000001602; 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:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
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; A4AVL1.
DR   SWISS-2DPAGE; A4AVL1.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|RuleBase:RU004517,
KW   ECO:0000313|EMBL:EAQ99941.1};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU004517};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|RuleBase:RU004517,
KW   ECO:0000313|EMBL:EAQ99941.1}.
FT   MOD_RES     121    121       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR006468-1}.
SQ   SEQUENCE   279 AA;  31313 MW;  1A678743C8112379 CRC64;
     MKAYKDEKDI VWLFRPLDNC KRLNVSAKRM AIPELPEDYF MDGLVELLNL EKDWIPQSAG
     SSLYIRPFIF ASGNGFHASP ADEYTFIIAC APSGAYFSGK VKVLIEEKYS RSANGGVGYA
     KAGGNYAGQF YPTQLAVEKG YNQVIWTDDN THEYIEEAGA MNIFVRINDT LITGPTSDRI
     LDGITRKSIL KIAKDEGIPF QVRKITVIEV VEAAKDGSLK EMFGAGTAAV ISPISTFGYR
     DTDYDLPEMP EGYATRLKKR ITDIQYNRSE DKFGWRYKV
//

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