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Database: UniProt
Entry: A0A254R9I9_9RHOB
LinkDB: A0A254R9I9_9RHOB
Original site: A0A254R9I9_9RHOB 
ID   A0A254R9I9_9RHOB        Unreviewed;       287 AA.
AC   A0A254R9I9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Probable branched-chain-amino-acid aminotransferase {ECO:0000256|ARBA:ARBA00014472};
GN   ORFNames=ATO6_07395 {ECO:0000313|EMBL:OWU86600.1};
OS   Oceanicola sp. 22II-s10i.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceanicola.
OX   NCBI_TaxID=1317116 {ECO:0000313|EMBL:OWU86600.1, ECO:0000313|Proteomes:UP000197567};
RN   [1] {ECO:0000313|EMBL:OWU86600.1, ECO:0000313|Proteomes:UP000197567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s10i {ECO:0000313|EMBL:OWU86600.1,
RC   ECO:0000313|Proteomes:UP000197567};
RA   Lai Q., Li G., Shao Z.;
RT   "Oceanicola sp. 22II-s10i Genome Sequencing.";
RL   Submitted (APR-2013) 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:OWU86600.1}.
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DR   EMBL; AQQU01000001; OWU86600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254R9I9; -.
DR   OrthoDB; 9805628at2; -.
DR   Proteomes; UP000197567; Unassembled WGS sequence.
DR   GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:RHEA.
DR   GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR   GO; GO:0052655; F:L-valine transaminase activity; IEA:RHEA.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd01558; D-AAT_like; 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; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF10; D-ALANINE AMINOTRANSFERASE; 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:OWU86600.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197567};
KW   Transferase {ECO:0000313|EMBL:OWU86600.1}.
SQ   SEQUENCE   287 AA;  31373 MW;  4893CED2559F3D95 CRC64;
     MSRTVYVNGD YLPEEEAKIS IFDRGFLMAD GVYEVTSVLG GKLIDFDGHA KRLERSLKEL
     DMAAPVTMDE LLAIHRELVA KNAIVDGAVY LQVTRGSAGD RDFAFPDPEK VPSSLVLFTQ
     SKPGMAYDPK VQKGISVISI DDIRWGRRDI KTVQLLYPSM GKMMAKAAGA DDAWMVEDGM
     VTEGTSNNAY IVKGGKIITR ALSNDILHGI TRAAVLRFAR EAQMEVEERS FSIDEAKDAD
     EAFITSASTF VMPVVKIDGA AVGEGKPGRV ALRLREIYLD ESCKAGI
//
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