ID A0A0M6YIF2_9RHOB Unreviewed; 456 AA.
AC A0A0M6YIF2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Omega-amino acid--pyruvate aminotransferase {ECO:0000313|EMBL:CTQ50138.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:CTQ50138.1};
GN ORFNames=JDO7802_02156 {ECO:0000313|EMBL:CTQ50138.1};
OS Jannaschia donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ50138.1, ECO:0000313|Proteomes:UP000049222};
RN [1] {ECO:0000313|EMBL:CTQ50138.1, ECO:0000313|Proteomes:UP000049222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ50138.1,
RC ECO:0000313|Proteomes:UP000049222};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CXSU01000012; CTQ50138.1; -; Genomic_DNA.
DR RefSeq; WP_055085418.1; NZ_CXSU01000012.1.
DR AlphaFoldDB; A0A0M6YIF2; -.
DR STRING; 420998.JDO7802_02156; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000049222; Unassembled WGS sequence.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF3; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:CTQ50138.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:CTQ50138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049222};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CTQ50138.1}.
SQ SEQUENCE 456 AA; 49293 MW; F838900E1128E536 CRC64;
MPDTSLPNSW DARAKAHSFF GFTDLPSIAE RGTVVLTHGE GPYVVDTDGT RYLDANSGLW
NMIAGFDHPD LTAAAQAQYA AFPGYHAFFG RMSDQAVMLS EKLVEVSPFE DGKVFYTNSG
SEANDTMVKM LWFLHGAEGR PQARKIITRG NAYHGVTAVS ASMTAKPYNA VFGLPLPGFL
HLTCPHYWRE GRDGESEAEF LARLVDELEQ MIATEGADTI AGFFAEPVQG AGGVIPPCDG
YFDAMLPVLR RHGIPIIADE VITGFGRTGA LWGCESYGFV PDAIISSKAL TAGFFPMGAV
ILGPELSDRL QRAVDVIEEF PHGFTASGHP VGCAIALKSI DLVMNGGLLN NVNHLIPTFE
AGLAKLAQHE HIGEWRGRGL MGALEAVRDK ATKTPFEGHL SVSERIANTC TDHGLICRPL
GQSIVLCPPF IMTDAQMEEM FDKLSRALNK VFAEVG
//