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Database: UniProt
Entry: A0A101KXY8_RHILI
LinkDB: A0A101KXY8_RHILI
Original site: A0A101KXY8_RHILI 
ID   A0A101KXY8_RHILI        Unreviewed;       220 AA.
AC   A0A101KXY8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Probable branched-chain-amino-acid aminotransferase {ECO:0000256|ARBA:ARBA00014472};
GN   ORFNames=AU467_00965 {ECO:0000313|EMBL:KUM29006.1};
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381 {ECO:0000313|EMBL:KUM29006.1, ECO:0000313|Proteomes:UP000053176};
RN   [1] {ECO:0000313|EMBL:KUM29006.1, ECO:0000313|Proteomes:UP000053176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM29006.1,
RC   ECO:0000313|Proteomes:UP000053176};
RA   Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA   Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT   "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT   efficient symbiont and plant-growth promoting strain isolated from Zn-
RT   mining soil using Leucaena leucocephala as a trap plant.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
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:KUM29006.1}.
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DR   EMBL; LPWA01000001; KUM29006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101KXY8; -.
DR   OrthoDB; 9809239at2; -.
DR   Proteomes; UP000053176; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SF24; AMINODEOXYCHORISMATE LYASE; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516}.
SQ   SEQUENCE   220 AA;  24129 MW;  130EBB63CCB1B3DF CRC64;
     MSSESALRDR NSADFELIET MRREPGSGFL RFDRHLARLY ASAAELGFAC DPQRVGEVLT
     GAVGGQRIAL RTRLALHRNG EAAASAQPYE PLPAGKAWRL QLARVRLDSG DTLLRHKTSR
     RDTYQRARAE YLATRADEVL LANERGELCE GTITNLFADF GDGVLATPRL DCGLLPGVLR
     AELLDEGRAM EAIYTFDDLK SAKAIFVGNS LRGLIPAQLA
//
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