ID   TPA_RHOCB               Reviewed;         459 AA.
AC   D5AKY0;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Taurine--pyruvate aminotransferase {ECO:0000250|UniProtKB:Q9APM5};
DE            EC=2.6.1.77 {ECO:0000250|UniProtKB:Q9APM5};
GN   Name=tpa {ECO:0000303|PubMed:17981966};
GN   OrderedLocusNames=RCAP_rcc02240 {ECO:0000312|EMBL:ADE85970.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   INDUCTION.
RC   STRAIN=B10S;
RX   PubMed=17981966; DOI=10.1128/jb.01510-07;
RA   Wiethaus J., Schubert B., Pfaender Y., Narberhaus F., Masepohl B.;
RT   "The GntR-like regulator TauR activates expression of taurine utilization
RT   genes in Rhodobacter capsulatus.";
RL   J. Bacteriol. 190:487-493(2008).
CC   -!- FUNCTION: Catalyzes the degradation of taurine into alanine and
CC       sulfoacetaldehyde. {ECO:0000250|UniProtKB:Q9APM5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyruvate + taurine = L-alanine + sulfoacetaldehyde;
CC         Xref=Rhea:RHEA:10420, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:58246, ChEBI:CHEBI:507393; EC=2.6.1.77;
CC         Evidence={ECO:0000250|UniProtKB:Q9APM5};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q9APM5};
CC   -!- PATHWAY: Organosulfur degradation; taurine degradation via aerobic
CC       pathway; acetyl phosphate and sulfite from taurine: step 1/2.
CC       {ECO:0000250|UniProtKB:Q9APM5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9APM5}.
CC   -!- INDUCTION: Induced by taurine via TauR. {ECO:0000269|PubMed:17981966}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CP001312; ADE85970.1; -; Genomic_DNA.
DR   RefSeq; WP_013067949.1; NC_014034.1.
DR   AlphaFoldDB; D5AKY0; -.
DR   SMR; D5AKY0; -.
DR   STRING; 272942.RCAP_rcc02240; -.
DR   EnsemblBacteria; ADE85970; ADE85970; RCAP_rcc02240.
DR   GeneID; 31491082; -.
DR   KEGG; rcp:RCAP_rcc02240; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_0_5; -.
DR   OMA; GHYWSGI; -.
DR   OrthoDB; 478143at2; -.
DR   UniPathway; UPA00336; UER00543.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..459
FT                   /note="Taurine--pyruvate aminotransferase"
FT                   /id="PRO_0000430552"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  49484 MW;  86BD2F75F2CFBAFC CRC64;
     MHAAPIPQDA APIIAADRAH VWHHLSQHKP YETSDPRVFV EGRGMRLWDA TGREFLDATS
     GGVWTVNLGY GRKDVVEAVA AQLLALPYYA GAAGTVPGAR YAEALIAKMP GLSRVYYSNS
     GSEANEKVYK MVRQISHRHH GGRKGKILFR ERDYHGTTIA ALATSGQAQR AEHYGPFPDG
     FVSVPHCLEY RAQWDCANYG ERAADAIEEV ILREGPDSIG CLVLEPITAG GGVIVPPAGY
     WEKVSHICRK YNILLHLDEV VCGLGRTGAW FGYQHYGIQP DFVTMAKGVA AGYAAISCTV
     TTEAVFELFK DAPSDPLCHF RDISTFGGCT AGPAAALETL RIIEEEGLLQ NTAQMGERLL
     ANLRDLAERH AVIGDVRGKG LFCGAELVAD RRTKEPLAEA KVQAVVADCA AQGVLIGATN
     RSIPGLNTTL CLAPALIASE AEIDRITETI DAALRRLAA