ID A0A0N8W522_9SPHI Unreviewed; 354 AA.
AC A0A0N8W522;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=branched-chain-amino-acid transaminase {ECO:0000256|ARBA:ARBA00013053};
DE EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN ORFNames=AQF98_18170 {ECO:0000313|EMBL:KQB99490.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQB99490.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQB99490.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQB99490.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) 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:KQB99490.1}.
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DR EMBL; LLWP01000009; KQB99490.1; -; Genomic_DNA.
DR RefSeq; WP_055133382.1; NZ_LLWP01000009.1.
DR AlphaFoldDB; A0A0N8W522; -.
DR STRING; 1740090.AQF98_18170; -.
DR OrthoDB; 9804984at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000050543; 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: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:KQB99490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050543};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQB99490.1}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 354 AA; 39067 MW; 5267EEEBFB1E79CD CRC64;
MIDTLQIKIT KNSNSRLAET EFKDIPFGKI FTDHMFVADF EDGEWKNFEI LPYGPIPMSP
AISALHYGQA IFEGMKAYRL PSGEISIFRA DKNFERFNIS ADRMAMPTIP EEIFMQGIAT
LINMDRDWVP TQENYALYLR PVMFATDDSL GVRASSNYKF VVLASPTGPY YTKALKVKIE
TKYTRANEGG VGYAKTAGNY ARSLYPFAQA QKEGFDQLIW TDSATHSFVE ESGAANVMFV
LDGKLITAAV GETILNGVTR DTIIALAKDK GITVEERKVT VAEIIAGAKN GTLTEAFAVG
TAATVTQIGE IGYEGELYQL SDSSTRTIST GIAKELNEIR NGLAADKFGW NWIV
//
