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Database: UniProt
Entry: A0A1D9M914_9RHOB
LinkDB: A0A1D9M914_9RHOB
Original site: A0A1D9M914_9RHOB 
ID   A0A1D9M914_9RHOB        Unreviewed;       456 AA.
AC   A0A1D9M914;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:AOZ68333.1};
GN   ORFNames=LPB142_02560 {ECO:0000313|EMBL:AOZ68333.1};
OS   Rhodobacter sp. LPB0142.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1850250 {ECO:0000313|EMBL:AOZ68333.1, ECO:0000313|Proteomes:UP000176562};
RN   [1] {ECO:0000313|EMBL:AOZ68333.1, ECO:0000313|Proteomes:UP000176562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0142 {ECO:0000313|EMBL:AOZ68333.1,
RC   ECO:0000313|Proteomes:UP000176562};
RA   Kim E., Yi H.;
RT   "Rhodobacter sp. LPB0142, isolated from sea water.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP017781; AOZ68333.1; -; Genomic_DNA.
DR   RefSeq; WP_071165425.1; NZ_CP017781.1.
DR   AlphaFoldDB; A0A1D9M914; -.
DR   STRING; 1850250.LPB142_02560; -.
DR   KEGG; rhp:LPB142_02560; -.
DR   Proteomes; UP000176562; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AOZ68333.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176562};
KW   Transferase {ECO:0000313|EMBL:AOZ68333.1}.
SQ   SEQUENCE   456 AA;  48241 MW;  CE2AAA6EDAAC3CEF CRC64;
     MGEALIGGVS IKRIEAFAAR EAAAYAAARP RTRAALAEGA GAFLDGVPMH WMRDWPQPFP
     MLVARARGAR IEDLDGHKID DFCLGDTGSM FGHSPAPVAR AIRAQAGRGL TYMLPTEDAL
     AAGRLLTERF GPMLWQIATT ATDANRNAIR VARAVTGRAK VLVFNGCYHG TVEDVMVRRR
     EGRTEARPGL VGQVADLTRL AVAAEFNDLA SVEAALAGGD IAAILTEPVM TNSCMVLPEP
     GFHAGLRDLA SRFGALLIID ETHTISSGLG GYTRTHGLEP DIFVTGKCVA GGVATAIWGL
     SRETARRFGV YDAARAPGHS GMGTTLSANP LQFAALRATL AEVMTPENYA RMEAGAARLS
     AGLTKAVTRV GAPWHVVRVG ARVEFICAPG PLKNGIEAEA AHKPALEAAI HQGLLNRGSL
     IAPFHNMMLI SPATSRAQID RLVAAFAEVL GQLFET
//
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