ID   XSC_DESTI               Reviewed;         584 AA.
AC   Q93PS3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Sulfoacetaldehyde acetyltransferase;
DE            EC=2.3.3.15;
GN   Name=xsc; Synonyms=sly;
OS   Desulfonispora thiosulfatigenes.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfonispora.
OX   NCBI_TaxID=83661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   PRELIMINARY CHARACTERIZATION.
RC   STRAIN=ATCC 700533 / DSM 11270 / GKNTAU;
RX   PubMed=11439112; DOI=10.1042/0264-6021:3570581;
RA   Denger K., Ruff J., Rein U., Cook A.M.;
RT   "Sulfoacetaldehyde sulfo-lyase [EC 4.4.1.12] from Desulfonispora
RT   thiosulfatigenes: purification, properties and primary sequence.";
RL   Biochem. J. 357:581-586(2001).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 700533 / DSM 11270 / GKNTAU;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q84H44};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:Q84H44};
CC   -!- PATHWAY: Organosulfur degradation; taurine degradation via aerobic
CC       pathway; acetyl phosphate and sulfite from taurine: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a sulfo-lyase.
CC       {ECO:0000305|PubMed:11439112}.
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DR   EMBL; AF305552; AAK66657.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93PS3; -.
DR   SMR; Q93PS3; -.
DR   PRIDE; Q93PS3; -.
DR   BioCyc; MetaCyc:MON-3662; -.
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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Direct protein sequencing; Magnesium;
KW   Metal-binding; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..584
FT                   /note="Sulfoacetaldehyde acetyltransferase"
FT                   /id="PRO_0000090845"
SQ   SEQUENCE   584 AA;  63939 MW;  43E5B50C2EEE8353 CRC64;
     MAKVKMTPSE AMTEVLVNEG VTHVTGILGS AFMDMLDLWP TAGIEFIAVR HEQTAGHMQD
     AYCRITGKAS VCIGQNGPGV TNLVTCVAAA NQAHTPMVVL GPSAGTPTVG WDGFQECDQV
     SIFRSITKQV LQVPHPSRAG DVLRTAFRIA YAERGPVYVD IPRNYFYGEV YEEILRPDQY
     RAMNVRGAGD ATELARATEI LAAAKNPVII SGRGVVDADA FAEVKEIAHM LTAPVAMSYL
     HNDTYPADDE LWVGPIGYMG AKSAMYSLQD ADVILAIGSR LSVFGTLPQY DINYFPENAK
     IIQIEVNPKQ IGRRHPVTVP IIGDAKLATA ELIKLLKAKG DVKPNAERLA KIQERRNDWF
     KEIEEMAMMP GNPINPRRVL FEVAKLMPED AILTTDIGNV ASTANSYFKF TKPKKHIAAL
     TFGNTGFAYQ AGLGAQMAEP DSPVVAIVGD GAWGQSLHEI STAVQYKLPV IACVFRNMAW
     CAEKKNQIDF YNNRFVGTEI PNPISFIPAA EAFGAKGIRV EKPEDIADAF KQGLAWRAEG
     HPVVLEFVVD GTILAPPFRK DALALPTRYL PKYEHLDAKY FPKN