ID   XSC_CASDE               Reviewed;         598 AA.
AC   Q84H44;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Sulfoacetaldehyde acetyltransferase {ECO:0000303|PubMed:12358600};
DE            EC=2.3.3.15 {ECO:0000269|PubMed:12358600};
GN   Name=xsc {ECO:0000303|PubMed:12358600};
OS   Castellaniella defragrans (Alcaligenes defragrans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Castellaniella.
OX   NCBI_TaxID=75697;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21; 211-230 AND
RP   303-314, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 11046 / CCUG 39541 / NKNTAU;
RX   PubMed=12358600; DOI=10.1042/bj20021455;
RA   Ruff J., Denger K., Cook A.M.;
RT   "Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification
RT   from Alcaligenes defragrans and gene clusters in taurine degradation.";
RL   Biochem. J. 369:275-285(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl phosphate + H(+) + sulfite = phosphate +
CC         sulfoacetaldehyde; Xref=Rhea:RHEA:24204, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58246; EC=2.3.3.15;
CC         Evidence={ECO:0000269|PubMed:12358600};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12358600};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:12358600};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.1 mM for sulfoacetaldehyde {ECO:0000269|PubMed:12358600};
CC         KM=6.4 mM for phosphate {ECO:0000269|PubMed:12358600};
CC         KM=2.2 uM for thiamine pyrophosphate {ECO:0000269|PubMed:12358600};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:12358600};
CC   -!- PATHWAY: Organosulfur degradation; taurine degradation via aerobic
CC       pathway; acetyl phosphate and sulfite from taurine: step 2/2.
CC       {ECO:0000269|PubMed:12358600}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12358600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12358600}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AY134843; AAN08489.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84H44; -.
DR   SMR; Q84H44; -.
DR   KEGG; ag:AAN08489; -.
DR   BioCyc; MetaCyc:MON-3001; -.
DR   BRENDA; 2.3.3.15; 229.
DR   UniPathway; UPA00336; UER00544.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050487; F:sulfoacetaldehyde acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019529; P:taurine catabolic process; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR017820; Sulphoacetald_Actrfrase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR03457; sulphoacet_xsc; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Direct protein sequencing; Magnesium;
KW   Metal-binding; Thiamine pyrophosphate; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12358600"
FT   CHAIN           2..598
FT                   /note="Sulfoacetaldehyde acetyltransferase"
FT                   /id="PRO_0000090843"
SQ   SEQUENCE   598 AA;  65108 MW;  37B9C9EF30BB6029 CRC64;
     MANDTRQVVQ GVQEMTPSEA FVETMVANGV TEIFGIMGSA FMDAMDIFAP AGIKLIPVVH
     EQGAAHMADG FARVSGRTGV VIGQNGPGIS NCVTAIAAAY WAHTPVVIVT PEAGTTGIGL
     GGFQEARQLP MFQEFTKYQG HVTHPARMAE YTARCFARAR DEMGPAQLNI PRDYFYGKIK
     CEIPLPQPLD RGPGGAQSLD AAARLLAEAK FPVIISGGGV VMGDAVEECK ALAERLGAPV
     VNSYLHNDSF PASHPLWCGP LGYQGSKAAM KLLADADVVL ALGTRLGPFG TLPQHGLDYW
     PKNARIIQVD ADSKMLGLVK KITVGVCGDA KASAAEISRR IDGMKLACDA NKAERAARIQ
     AEKDAWEQEL TDWTHERDPF SLDMIEEQSK EEGNWLHPRQ VLRELEKAMP EDVMVSTDIG
     NINSVANSYL RFEKPRSFFA AMSWGNCGYA FPTIIGAKVA APHRPAVSYA GDGAWGMSMS
     EIMTCVRHDI PVTAVVFHNR QWGAEKKNQV DFYNRRFVAG ELESESFAGI ARAMGAEGVV
     VDRIEDVGPA LKKAIDAQMN DRKTTVIEIM CTRELGDPFR RDALSKPVRL LEKYRDYT