ID A0A2P8FKF5_9RHOB Unreviewed; 287 AA.
AC A0A2P8FKF5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=CLV88_101628 {ECO:0000313|EMBL:PSL22203.1};
OS Shimia abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL22203.1, ECO:0000313|Proteomes:UP000240418};
RN [1] {ECO:0000313|EMBL:PSL22203.1, ECO:0000313|Proteomes:UP000240418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL22203.1,
RC ECO:0000313|Proteomes:UP000240418};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109}.
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 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 -!- 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:PSL22203.1}.
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DR EMBL; PYGJ01000001; PSL22203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8FKF5; -.
DR OrthoDB; 21319at2; -.
DR Proteomes; UP000240418; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
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 Aminotransferase {ECO:0000313|EMBL:PSL22203.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000240418};
KW Transferase {ECO:0000313|EMBL:PSL22203.1}.
SQ SEQUENCE 287 AA; 31853 MW; 4C02E0DEC5ACE831 CRC64;
MAVGTNIRTF FNNSWHDGDI SVMRAADHGS WLGTTVFDGA RFFDGVMPDL DRHCARVNRS
AEALMLAPTV STDDMVDIIR EGLKTFDKDA AVYIRPMYWG IGGDITAIIP SQEETGFAIC
LEQIPMAPPE ASATLTRTRF RRPVLEDAVV NAKAGCLYPN NARMLAEARQ KGFSNALVTD
ALGNVAETAT ANIFMVRDGE VFTPIPNGTF LAGITRARHI ENMRADGLKV HETVLSFADF
EAADEVFMSG NMNKVTPIKA FDDRQYQHGP VTRRAREMYW DWAHSRV
//
