ID   XSC_RHIME               Reviewed;         591 AA.
AC   Q92UW6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Probable sulfoacetaldehyde acetyltransferase;
DE            EC=2.3.3.15;
GN   Name=xsc; OrderedLocusNames=RB0970; ORFNames=SMb21530;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AL591985; CAC49370.1; -; Genomic_DNA.
DR   PIR; B95963; B95963.
DR   RefSeq; NP_437510.1; NC_003078.1.
DR   RefSeq; WP_010975814.1; NC_003078.1.
DR   AlphaFoldDB; Q92UW6; -.
DR   SMR; Q92UW6; -.
DR   STRING; 266834.SM_b21530; -.
DR   PRIDE; Q92UW6; -.
DR   EnsemblBacteria; CAC49370; CAC49370; SM_b21530.
DR   GeneID; 61600935; -.
DR   KEGG; sme:SM_b21530; -.
DR   PATRIC; fig|266834.11.peg.5897; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OMA; DGGFLMG; -.
DR   UniPathway; UPA00336; UER00544.
DR   Proteomes; UP000001976; Plasmid pSymB.
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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Magnesium; Metal-binding; Plasmid;
KW   Reference proteome; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..591
FT                   /note="Probable sulfoacetaldehyde acetyltransferase"
FT                   /id="PRO_0000090846"
FT   REGION          359..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  64157 MW;  7234D44FB221EB97 CRC64;
     MKMTTEEAFV KVLQMHGIEH AFGIIGSAMM PVSDLFPKAG IRFWDCAHET NAGMMADGFS
     RATGTMSMAI GQNGPGVTGF ITAMKTAYWN HTPLLMVTPQ AANKTIGQGG FQEVDQMAMF
     EEMVCYQEEV RDPSRIPEVL NRVIEKAWRG CAPAQINIPR DFWTQVIDVD LPRIVRFERP
     AGGPAAIAQA ARLLSEAKFP VILNGAGVVI GNAIQESMAL AEKLDAPVCC GYQHNDAFPG
     SHRLSVGPLG YNGSKAAMEL ISKADVVLAL GTRLNPFSTL PGYGIDYWPK DAAIIQVDIN
     ADRIGLTKKV TVGICGDAKQ VAQQILQQLA PAAGDASREE RKALVHQTRS AWLQQLSSMD
     HEDDDPGTEW NVGARQREPD RMSPRQVWRA IQAVLPKEAI ISTDIGNNCA IGNAYPSFEQ
     GRKYLAPGMF GPCGYGFPSI VGAKIGCPDV PVVGFAGDGA FGISMNEMTS IGREGWPAIT
     MVIFRNYQWG AEKRNTTLWY DNNFVGTELN PNLSYAKVAD GCGLKGVTVD TPAALTEALA
     KAIEDQAKGI TTFVEVVLNQ ELGEPFRRDA MKKPVAVAGI DRADMRTQRR M