ID   HTPA_PARDP              Reviewed;         459 AA.
AC   A1B9Z3;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Hypotaurine/taurine--pyruvate aminotransferase {ECO:0000305};
DE            Short=Hpa/Tpa {ECO:0000303|PubMed:23603744};
DE            EC=2.6.1.77 {ECO:0000269|PubMed:23603744};
GN   Name=hpa/tpa {ECO:0000303|PubMed:23603744};
GN   OrderedLocusNames=Pden_4273 {ECO:0000312|EMBL:ABL72337.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, INDUCTION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Pd 1222;
RX   PubMed=23603744; DOI=10.1128/jb.00307-13;
RA   Felux A.K., Denger K., Weiss M., Cook A.M., Schleheck D.;
RT   "Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination
RT   followed by spontaneous desulfination to yield acetaldehyde and, finally,
RT   acetate for growth.";
RL   J. Bacteriol. 195:2921-2930(2013).
CC   -!- FUNCTION: Converts hypotaurine to alanine and sulfinoacetaldehyde,
CC       which desulfinates spontaneously to acetaldehyde and sulfite. Can also
CC       catalyze the degradation of taurine into alanine and sulfoacetaldehyde,
CC       which is stable (PubMed:23603744). Has 2-fold higher aminotransferase
CC       activity with hypotaurine as the substrate (PubMed:23603744).
CC       {ECO:0000269|PubMed:23603744}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hypotaurine + pyruvate = 2-sulfinoacetaldehyde + L-alanine;
CC         Xref=Rhea:RHEA:58056, ChEBI:CHEBI:15361, ChEBI:CHEBI:57853,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:142501; EC=2.6.1.77;
CC         Evidence={ECO:0000269|PubMed:23603744};
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:0000269|PubMed:23603744};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:23603744};
CC   -!- PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:23603744}.
CC   -!- INDUCTION: Induced by growth on hypotaurine.
CC       {ECO:0000269|PubMed:23603744}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CP000490; ABL72337.1; -; Genomic_DNA.
DR   RefSeq; WP_011750502.1; NC_008687.1.
DR   AlphaFoldDB; A1B9Z3; -.
DR   SMR; A1B9Z3; -.
DR   STRING; 318586.Pden_4273; -.
DR   PRIDE; A1B9Z3; -.
DR   EnsemblBacteria; ABL72337; ABL72337; Pden_4273.
DR   KEGG; pde:Pden_4273; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_0_5; -.
DR   OMA; HCMEYRK; -.
DR   BioCyc; MetaCyc:MON-18238; -.
DR   BRENDA; 2.6.1.77; 3341.
DR   Proteomes; UP000000361; Chromosome 2.
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   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..459
FT                   /note="Hypotaurine/taurine--pyruvate aminotransferase"
FT                   /id="PRO_0000446013"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12995"
SQ   SEQUENCE   459 AA;  50395 MW;  90B56008AD6B90ED CRC64;
     MTLDLNPNDM SHVVAADRAH VWHHLSQHKQ YETIDPRVFV EGKGMRLWDA TGREFLDAVS
     GGVWTVNVGY GRESIADAIR DQLVKLNYYA GAAGTVPGAI FAQKLIEKMP GMTRVYYSNS
     GSEANEKVYK MVRQIAARHH GGKKWKILYR DRDYHGTTIA TLATSGQDQR AIAYGPFPDG
     FVRVPHCLEY RKQWDVENYG ERAADAIEEV ILREGPDTVG AIVLEPVTAG GGVITPPEGY
     WQRVQEICRK YDILLHIDEV VCGLGRTGTW FGYQQYGIEP DFVTMAKGVA SGYAAISCTV
     TTERVFEMFK DAPEDGMSFF RDISTFGGCT SGPVAAIENM RIIEDEGLLD NTVAMGERTL
     ANLNALMEKH KVIGDVRGKG LFCGAELVAD RASKEPMDEK KVQAVVADCL AQGVIIGATN
     RSLPGFNNTL CLSPALIATA DNIDRITDAI DNALTKVFA