UniProt: A0A223V1D3

Database: UniProt
Entry: A0A223V1D3_9FLAO

LinkDB:  A0A223V1D3_9FLAO 
Original site:  A0A223V1D3_9FLAO

All links

Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (7)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

Download RDF

ID   A0A223V1D3_9FLAO        Unreviewed;       358 AA.
AC   A0A223V1D3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   ORFNames=CJ263_02265 {ECO:0000313|EMBL:ASV29141.1}, GCM10011412_06440
GN   {ECO:0000313|EMBL:GGD71578.1};
OS   Maribacter cobaltidurans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1178778 {ECO:0000313|EMBL:ASV29141.1, ECO:0000313|Proteomes:UP000215244};
RN   [1] {ECO:0000313|EMBL:ASV29141.1, ECO:0000313|Proteomes:UP000215244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:ASV29141.1,
RC   ECO:0000313|Proteomes:UP000215244};
RA   Wu Y.-H., Cheng H., Xu X.-W.;
RT   "The complete genome sequence of Maribacter sp. B1, isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GGD71578.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD71578.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GGD71578.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD71578.1};
RA   Sun Q., Zhou Y.;
RL   Submitted (DEC-2022) 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         ECO:0000256|RuleBase:RU004517};
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         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; EC=2.6.1.42;
CC         Evidence={ECO:0000256|ARBA:ARBA00001745,
CC         ECO:0000256|RuleBase:RU004517};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
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       ECO:0000256|RuleBase:RU004106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP022957; ASV29141.1; -; Genomic_DNA.
DR   EMBL; BMJL01000001; GGD71578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223V1D3; -.
DR   KEGG; marb:CJ263_02265; -.
DR   OrthoDB; 9804984at2; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000215244; Chromosome.
DR   Proteomes; UP000603042; 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; IPR018300; Aminotrans_IV_CS.
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.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU004517};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215244};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004517}.
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   358 AA;  40153 MW;  0B1BFCF41777E356 CRC64;
     MSVETKKVNI SVERAKTSKI NQVDFDNLKF GSVYTDHMLV CDYKNGVWEA PKIMPYQQIM
     LDPSAKVFHY GQSIFEGMKA YKDDNGSIFL FRPLDNHKRL NISAKRLSIP ELPEEYFMEG
     LTTLLELDSD FIPTKEGSSL YIRPFMFASG NGFHASPADE YKFIIACAPS GSYFSGKVKV
     LIEQTYSRSA NGGVGFAKAG GNYAGQFYPT QLAIEKGYNQ VIWTDDTEHE YIEEAGAMNI
     FIRINDTLIT GPTSDRILDG ITRKSILEIA KDNSIPTEVR KITVTEVVNA AKDGSLKEMF
     GAGTAAVISP ISAFGYKDKD YDLPELENSY ASKLKKLITD IQYNKSEDKY GWRFMVKS
//

DBGET integrated database retrieval system