ID   A0A0N7LNH7_9RHOB        Unreviewed;       591 AA.
AC   A0A0N7LNH7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   Name=xsc {ECO:0000313|EMBL:CUH42452.1};
GN   ORFNames=RUA4292_04717 {ECO:0000313|EMBL:CUH50508.1}, RUM4293_01340
GN   {ECO:0000313|EMBL:CUH42452.1};
OS   Ruegeria atlantica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=81569 {ECO:0000313|EMBL:CUH42452.1, ECO:0000313|Proteomes:UP000050786};
RN   [1] {ECO:0000313|Proteomes:UP000050783, ECO:0000313|Proteomes:UP000050786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4292 {ECO:0000313|EMBL:CUH50508.1,
RC   ECO:0000313|Proteomes:UP000050783}, and CECT 4293
RC   {ECO:0000313|EMBL:CUH42452.1, ECO:0000313|Proteomes:UP000050786};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CYPS01000022; CUH42452.1; -; Genomic_DNA.
DR   EMBL; CYPU01000074; CUH50508.1; -; Genomic_DNA.
DR   RefSeq; WP_058272524.1; NZ_CYPU01000074.1.
DR   AlphaFoldDB; A0A0N7LNH7; -.
DR   STRING; 81569.RUM4293_01340; -.
DR   GeneID; 55495834; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000050783; Unassembled WGS sequence.
DR   Proteomes; UP000050786; 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   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
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_TPP-bd.
DR   NCBIfam; TIGR03457; sulphoacet_xsc; 1.
DR   PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:CUH42452.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH42452.1}.
FT   DOMAIN          3..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..324
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   591 AA;  63108 MW;  892EA7BD58DD1940 CRC64;
     MKMTTEEAFV KVLQMHGIEH AFGIIGSAMM PISDIFPAAG INFWDCAHEG SGGMMADGYT
     RATGKMSMMI AQNGPGITNF VTAVKTAYWN HTPVLLITPQ AANKTIGQGG FQEMEQMRMF
     ADCVAYQEEL RDPSRVAEVL NRVILQAKRA SAPAQMNIPR DMWTQVIDVE LPKIVEFAAT
     AGGNEALDEA AALLSDAKFP VILNGAGVVL SGAIPASADL AERLTAPVCV GYQHNDAFPG
     SHPLFAGPLG YNGSKAGMEL IAKADVVLAL GTRLNPFSTL PGYGINYWPT DAKIIQVDLN
     PDRIGLTKDV TVGIVGDAKK VAEGLLERLG DNAGEAGRED RKNLIATTKS AWAQELSSLT
     HENDDPGTTW NERARAAKPD WMSPRMAWRA IQAALPTEAI ISSDIGNNCA IGNAYPSFEE
     GRKYLAPGLF GPCGYGLPAV VGAKIGCPDV PVVGFSGDGA FGIAVNELTA IGREEWPAVT
     QIVFRNYQWG AEKRNSTLWF DDNFVGTELD QQVSYAGIAT ACGLKGVVAR TQDELTAALN
     QAIIDQKNGI TTLIEAMINQ ELGDPFRRDA MKKPVRVAGI DAADMNTSAG A
//