ID   A0A0R0CU00_9GAMM        Unreviewed;       457 AA.
AC   A0A0R0CU00;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Beta-alanine--pyruvate transaminase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ABB29_08375 {ECO:0000313|EMBL:KRG69802.1};
OS   Pseudoxanthomonas dokdonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG69802.1, ECO:0000313|Proteomes:UP000052052};
RN   [1] {ECO:0000313|EMBL:KRG69802.1, ECO:0000313|Proteomes:UP000052052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG69802.1,
RC   ECO:0000313|Proteomes:UP000052052};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KRG69802.1}.
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DR   EMBL; LDJL01000008; KRG69802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R0CU00; -.
DR   STRING; 344882.ABB29_08375; -.
DR   PATRIC; fig|344882.3.peg.3029; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000052052; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; IPR049704; Aminotrans_3_PPA_site.
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:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   457 AA;  49277 MW;  0D7F9BDB549E2EBB CRC64;
     MSPDPAATTA LADYYQQQAT AKPASMDAFW MPFTANKQFK AAPRLLASAS GMHYRDVDGR
     EILDACAGLW CVNAGHARPR IVEAVKRQIE TLDFAPNFSM SSPLPFVLAQ RLAELSPGDL
     NHVFFTNSGS ESVDSALKIA LAYHRARGDG QRTRLIGREK AYHGVGFGGI SVGGLPNNRK
     WFGPLLPGTD HLRHTLDIQR NAFSQGLPAH GLELAEDLER LVALHDASTI AAVIIEPISG
     SAGVILPPDG YLQRIRQICD KHGILLIFDE VITGFGRVGK AFAAQRVGVT PDIITAAKGL
     SNGCVPMGAV LVSERIHQAF AQGADNAIDL FHGYTYSGHP LACAAALATL DTYAEENLFE
     KAIELGDYWQ QAIHSLKGLP NVIDIRNYGL IGAIEFAPRD GAPGTRGFDV FNDAFHKGGM
     LTRVTGDVIA LSPPLIIEKT HIDQIFERLA DIIRGVA
//