ID A0A1J5TY06_9GAMM Unreviewed; 309 AA.
AC A0A1J5TY06;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|ARBA:ARBA00018179, ECO:0000256|RuleBase:RU364094};
DE Short=BCAT {ECO:0000256|RuleBase:RU364094};
DE EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053, ECO:0000256|RuleBase:RU364094};
GN Name=ilvE {ECO:0000256|RuleBase:RU364094};
GN ORFNames=BGC33_15295 {ECO:0000313|EMBL:OIR25739.1}, MS2017_1134
GN {ECO:0000313|EMBL:AYQ56836.1};
OS Bathymodiolus thermophilus thioautotrophic gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2360 {ECO:0000313|EMBL:OIR25739.1, ECO:0000313|Proteomes:UP000182798};
RN [1] {ECO:0000313|Proteomes:UP000182798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAT/CrabSpa'14 {ECO:0000313|Proteomes:UP000182798};
RA Ponnudurai R., Kleiner M., Sayavedra L., Thuermer A., Felbeck H.,
RA Schlueter R., Schweder T., Markert S.;
RT "Genome Sequence of Bathymodiolus thermophilus sulfur-oxidizing gill
RT endosymbiont.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIR25739.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BAT/CrabSpa'14 {ECO:0000313|EMBL:OIR25739.1};
RX PubMed=28878861; DOI=10.1186/s40793-017-0266-y;
RA Ponnudurai R., Sayavedra L., Kleiner M., Heiden S.E., Thurmer A.,
RA Felbeck H., Schluter R., Sievert S.M., Daniel R., Schweder T., Markert S.;
RT "Genome sequence of the sulfur-oxidizing Bathymodiolus thermophilus gill
RT endosymbiont.";
RL Stand. Genomic Sci. 12:50-50(2017).
RN [3] {ECO:0000313|EMBL:AYQ56836.1, ECO:0000313|Proteomes:UP000278334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR9N {ECO:0000313|EMBL:AYQ56836.1,
RC ECO:0000313|Proteomes:UP000278334};
RA Won Y.-J.;
RT "Genome sequence of the bacterial symbiont EPR9N from a vent mussel
RT Bathymodiolus thermophilus.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109, ECO:0000256|RuleBase:RU364094}.
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:RU364094};
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: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; EC=2.6.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00001745,
CC ECO:0000256|RuleBase:RU364094};
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, ECO:0000256|RuleBase:RU364094}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000256|ARBA:ARBA00005072,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC ECO:0000256|RuleBase:RU004106}.
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DR EMBL; CP024634; AYQ56836.1; -; Genomic_DNA.
DR EMBL; MIQH01000001; OIR25739.1; -; Genomic_DNA.
DR RefSeq; WP_071563173.1; NZ_MIQH01000001.1.
DR AlphaFoldDB; A0A1J5TY06; -.
DR KEGG; bthg:MS2017_1134; -.
DR OrthoDB; 21319at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000182798; Unassembled WGS sequence.
DR Proteomes; UP000278334; 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 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; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR NCBIfam; TIGR01122; ilvE_I; 1.
DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42743:SF20; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-LIKE PROTEIN 2; 1.
DR Pfam; PF01063; Aminotran_4; 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:RU364094};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU364094};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364094}.
SQ SEQUENCE 309 AA; 34722 MW; 82AF0D0F9EE0E378 CRC64;
MSGFEDRDGL IWFDGKWVDW RDAKVHVLTH TLHYGMGVFE GVRAYQTDQG AAIFRLEEHT
NRLFNSAKIM NMNIGFSKEE INQAQRDSVA KNNLDSAYIR PMCFYGSEGM GLRADNLKVH
TIVAAWEWGS YLGEDNMKNG LRIRTSSYMR HHVNISMTKA KANGNYINSM LALQEALTDG
YDEALLLDVD GFVAEGSGEN IFIVRDGVIY TPDLTSALAG ITRDTIFTLA SGLGYKVIEK
RITRDEVYCA DEAFFTGTAA EVTPIRELDN RAIGTGTRGP ITEQLQSLYF DCVYGRNKQY
QHWIAKGSC
//
