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Database: UniProt
Entry: A0A1E5AJA5_9RHOB
LinkDB: A0A1E5AJA5_9RHOB
Original site: A0A1E5AJA5_9RHOB 
ID   A0A1E5AJA5_9RHOB        Unreviewed;       286 AA.
AC   A0A1E5AJA5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Probable branched-chain-amino-acid aminotransferase {ECO:0000256|ARBA:ARBA00014472};
GN   ORFNames=AB838_02265 {ECO:0000313|EMBL:OED50348.1};
OS   Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED50348.1, ECO:0000313|Proteomes:UP000094333};
RN   [1] {ECO:0000313|EMBL:OED50348.1, ECO:0000313|Proteomes:UP000094333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB1-7 {ECO:0000313|EMBL:OED50348.1};
RX   PubMed=27681823; DOI=10.1038/srep34362;
RA   Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT   "Single sample resolution of rare microbial dark matter in a marine
RT   invertebrate metagenome.";
RL   Sci. Rep. 6:34362-34362(2016).
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:OED50348.1}.
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DR   EMBL; MDLF01000032; OED50348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5AJA5; -.
DR   STRING; 1868286.AB838_02265; -.
DR   Proteomes; UP000094333; 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   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:OED50348.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516}; Transferase {ECO:0000313|EMBL:OED50348.1}.
SQ   SEQUENCE   286 AA;  31666 MW;  D873AA06814FD0D4 CRC64;
     MTRTVYVNGE YLPENEAKVS IFDRGFLFAD AVYEVTSVLD GKLIDFEGHA VRLERSLNEL
     DMPSPCTKDE LLEIHRKLVE LNGIEEGLVY LQVSRGSDGD RDFVFPSADT PPSLVLFTQN
     KPGLADSPAA KKGAKIISIE DIRWGRRDIK TVQLLYPSMG KMMAKKAGCD DAWLIEDGHV
     TEGTSNNAYY VKNGKIVTRP LSNDILHGIT RAAVLRLAEE AQMEIEERLF TIDEAKEADE
     AFTTSASAFV MPVVEIDGVA LGDGTPGPIA KRLREIYLEE SRKKAV
//
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