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Entry: A0A2A4B649_9SPHN
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ID   A0A2A4B649_9SPHN        Unreviewed;       367 AA.
AC   A0A2A4B649;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Probable branched-chain-amino-acid aminotransferase {ECO:0000256|ARBA:ARBA00014472};
DE            EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN   ORFNames=COC42_03430 {ECO:0000313|EMBL:PCD04673.1};
OS   Sphingomonas spermidinifaciens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1141889 {ECO:0000313|EMBL:PCD04673.1, ECO:0000313|Proteomes:UP000218366};
RN   [1] {ECO:0000313|EMBL:PCD04673.1, ECO:0000313|Proteomes:UP000218366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9NM-10 {ECO:0000313|EMBL:PCD04673.1,
RC   ECO:0000313|Proteomes:UP000218366};
RA   Feng G., Zhu H.;
RT   "Sphingomonas spermidinifaciens 9NM-10, whole genome shotgun sequence.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC         L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC         Evidence={ECO:0000256|ARBA:ARBA00000627};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC         glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC         Evidence={ECO:0000256|ARBA:ARBA00000995};
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; EC=2.6.1.42;
CC         Evidence={ECO:0000256|ARBA:ARBA00001745};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004824}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00005072}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCD04673.1}.
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DR   EMBL; NWMW01000001; PCD04673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4B649; -.
DR   OrthoDB; 9804984at2; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000218366; Unassembled WGS sequence.
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:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
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   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR033939; BCAT_family.
DR   NCBIfam; TIGR01123; ilvE_II; 1.
DR   PANTHER; PTHR11825:SF44; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:PCD04673.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218366};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PCD04673.1}.
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   367 AA;  39807 MW;  39A7CAE1DB5EA486 CRC64;
     MTPTLDVTTT FPLERHASPV DATTRAGLLE NPGFGRIFTD HMAVARWNAE KGWHDLAIQP
     RASLQMDPAC AVLHYAQEIF EGLKAYRTDD GGVTLFRADA NARRFRESAR RMAMAELPED
     LFLASIDALV AADREWIPAI EGGSLYLRPF MIASEVFLGV KPSAEYLYMV IASPAGAYFK
     GSAPSITVWV SEDYTRAAPG GTGAAKCGGN YAASLQAQAE AIREGCDQVV FLDAVQRAEV
     EELGGMNTFF VFDDGSIQTP PLTGTILPGI TRDSILTLAR DEGLGVREAP YSIDAWEADA
     ASGRLRESFA CGTAAVVTPI GRVRGRSRDF RIGNGGPGEL TSRLRERLVA IQKQQAPDPH
     GWVRRIL
//
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