ID   A0A1M6Q144_9PROT        Unreviewed;       441 AA.
AC   A0A1M6Q144;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Beta-alanine--pyruvate transaminase {ECO:0000313|EMBL:SHK13893.1};
GN   ORFNames=SAMN02745194_04272 {ECO:0000313|EMBL:SHK13893.1};
OS   Roseomonas rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Roseomonas.
OX   NCBI_TaxID=198092 {ECO:0000313|EMBL:SHK13893.1, ECO:0000313|Proteomes:UP000184387};
RN   [1] {ECO:0000313|EMBL:SHK13893.1, ECO:0000313|Proteomes:UP000184387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14916 {ECO:0000313|EMBL:SHK13893.1,
RC   ECO:0000313|Proteomes:UP000184387};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQZF01000033; SHK13893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6Q144; -.
DR   STRING; 198092.SAMN02745194_04272; -.
DR   Proteomes; UP000184387; 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; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:SHK13893.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   441 AA;  47477 MW;  2BFBD91FC108694B CRC64;
     MNEMSLPRPN NLDSFWMPYS DNRYFKQNPR MLARAEGMSY YTPEGREVLD GTAGLWCCNA
     GHGRREIVEA IQKQAALMDF APTFQLGHPI AFEAAARVAE MTPAGIDKVF FTNSGSESAD
     TALKIALAYQ KARGQSQRVR LIGRERGYHG VGFGGMSVGG IGGNRKQFGA MLPYVDHLPH
     THDPKRNAFA KGQPEHGIEL ADRLEDLVAL HGDTIAAVMV EPVAGSTGVL VPPTGYLQRL
     RELCDKHGIL LIFDEVITGF GRLGTDFGAE RLGVTPDIMT MAKGLTNAAV PMGAVATSNE
     VFDTVVNGSP AGIELFHGYT YSGHPLASAA AIATLALHRE EDLPGRARAI EPYWQEAAHS
     LSSAPGVVDI RDFGLIAGIE LAPREGKPGA RAMDVFRKCF DDGVLIRVTG DIIALSPPLI
     VEKPHVDRIM GTLSDAIHAI A
//