ID   XSC_ROSNI               Reviewed;         603 AA.
AC   A3SR25;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Sulfoacetaldehyde acetyltransferase {ECO:0000303|PubMed:19581363};
DE            EC=2.3.3.15 {ECO:0000269|PubMed:19581363};
GN   Name=xsc {ECO:0000303|PubMed:19581363};
GN   ORFNames=ISM_10690 {ECO:0000312|EMBL:EAP75048.1};
OS   Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=89187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM;
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM;
RX   PubMed=19581363; DOI=10.1128/jb.00569-09;
RA   Denger K., Mayer J., Buhmann M., Weinitschke S., Smits T.H., Cook A.M.;
RT   "Bifurcated degradative pathway of 3-sulfolactate in Roseovarius
RT   nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate
RT   sulfolyase.";
RL   J. Bacteriol. 191:5648-5656(2009).
CC   -!- FUNCTION: Catalyzes the degradation of sulfoacetaldehyde into sulfite
CC       and acetyl phosphate. Involved in sulfolactate degradation.
CC       {ECO:0000269|PubMed:19581363}.
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:19581363};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24206;
CC         Evidence={ECO:0000269|PubMed:19581363};
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   -!- INDUCTION: Induced during growth on sulfolactate or taurine.
CC       {ECO:0000269|PubMed:19581363}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AALY01000004; EAP75048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3SR25; -.
DR   SMR; A3SR25; -.
DR   STRING; 89187.ISM_10690; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   BioCyc; MetaCyc:MON-15909; -.
DR   BRENDA; 2.3.3.15; 10365.
DR   Proteomes; UP000005954; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..603
FT                   /note="Sulfoacetaldehyde acetyltransferase"
FT                   /id="PRO_0000445999"
SQ   SEQUENCE   603 AA;  65061 MW;  51ABFAD0358BEA7C CRC64;
     MLFRASQPED KPMKMTTEEA FVKTLQMHGI QHAFGIIGSA MMPISDIFGK AGITFWDCAH
     EGSGGMMADG YTRATGKMSM MIAQNGPGIT NFVTAVKTAY WNHTPLLLVT PQAANKTMGQ
     GGFQEVEQMA AFKDMVCYQE EVRDPTRMAE VLNRVILNAK RYSAPAQINV PRDYFTQVID
     IELPKIVDFE RPSGGEEALD EAAKLLSEAK FPVILNGAGV ILAGAIPATA ELAERLDAPV
     CCGYQHNDAF PGSHPLHAGP LGYNGSKAGM ELISKADVVL ALGTRLNPFS TLPGYGIDYW
     PKDAKIIQVD VKPERIGLTK PVAVGIVGDA KKVAKTILAK LSDTAGDADR EERKATIAKT
     KSAWAQELSS MDHEQDDPGT TWNERARGAK PDWMSPRMAW RAIQAALPKE AIISSDIGNN
     CAIGNAYPSF EEGRKYLAPG LFGPCGYGLP AVVGAKIGCP DTPVVGFSGD GAFGIAVNEL
     TAIGRGEWPA VTHVVFRNYQ WGAEKRNSTL WFDDNFVGTE LDEQVSYAGI AKACGLKGVV
     ARTMDELTDA LDQAIKDQKA GTTTLIEAMI NQELGEPFRR DAMKKPVAVA GIDPADMREQ
     QVD