ID   XSC_RHOCB               Reviewed;         590 AA.
AC   D5AKX8;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Sulfoacetaldehyde acetyltransferase {ECO:0000250|UniProtKB:Q84H44};
DE            EC=2.3.3.15 {ECO:0000250|UniProtKB:Q84H44};
GN   Name=xsc {ECO:0000303|PubMed:17981966};
GN   OrderedLocusNames=RCAP_rcc02238 {ECO:0000312|EMBL:ADE85968.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   INDUCTION.
RC   STRAIN=B10S;
RX   PubMed=17981966; DOI=10.1128/jb.01510-07;
RA   Wiethaus J., Schubert B., Pfaender Y., Narberhaus F., Masepohl B.;
RT   "The GntR-like regulator TauR activates expression of taurine utilization
RT   genes in Rhodobacter capsulatus.";
RL   J. Bacteriol. 190:487-493(2008).
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:0000250|UniProtKB:Q84H44};
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       {ECO:0000250|UniProtKB:Q84H44}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q84H44}.
CC   -!- INDUCTION: Induced by taurine via TauR. {ECO:0000269|PubMed:17981966}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; CP001312; ADE85968.1; -; Genomic_DNA.
DR   RefSeq; WP_013067947.1; NC_014034.1.
DR   AlphaFoldDB; D5AKX8; -.
DR   SMR; D5AKX8; -.
DR   STRING; 272942.RCAP_rcc02238; -.
DR   PRIDE; D5AKX8; -.
DR   EnsemblBacteria; ADE85968; ADE85968; RCAP_rcc02238.
DR   GeneID; 31491080; -.
DR   KEGG; rcp:RCAP_rcc02238; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OMA; MATCGEV; -.
DR   OrthoDB; 391134at2; -.
DR   UniPathway; UPA00336; UER00544.
DR   Proteomes; UP000002361; Chromosome.
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   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..590
FT                   /note="Sulfoacetaldehyde acetyltransferase"
FT                   /id="PRO_0000430553"
SQ   SEQUENCE   590 AA;  63258 MW;  66CDFDA6E2759F9F CRC64;
     MRMTTEEAFV KVLQRHGIDT AFGIIGSAFM PISDLFPRAG IRFFDCAHEG SGGMMADGFT
     RASGRMAMII AQNGPGVTNF VTAVKTAYWN HTPMLVVTPQ AANRTIGQGG FQEVEQMALF
     RDMVCWQEEL RDPARIAEVL DRVIRKARRA SAPAQINLPR DMFTKIIDIE LPQGVDLPRP
     APDAQALDRA AALLSSARFP VILNGAGVVL AEAIPDTVAL AERLEAPVCT GYQHNDAFPG
     SHPLFAGPLG YNGSKAAMQL MSQADVVLCL GTRLNPFSTL PGYGIDYWPK AAAVIQVDIN
     PDRIGLTRPV TLGIAADAGA VARGILARLG AQAGDQDRAE RAARIATTKS RWAQELASMD
     HEEDDPGTSW NERARAAKPG WMSPRMAWRA ITAALPPEAI LSSDIGNNCA IGNAYPSFAA
     GRKYLAPGLF GPCGYGLPAI IGAKIACPET PVVGFAGDGA FGISVTELTA IGRADWPAIT
     MVVFRNYQWG AEKRNSTLWY DDNFVGTELD LQVSYAGIAQ ACGLQGVVAR TMEELTEALR
     KALADQAAGK TTLIEALINQ ELGEPFRRDA MTKPVVVAGI DPADMRPQPR