ID   A0A1W6BCW5_9PROT        Unreviewed;       594 AA.
AC   A0A1W6BCW5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   ORFNames=B5L73_02760 {ECO:0000313|EMBL:ARJ47730.1};
OS   Candidatus Pelagibacter sp. RS39.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae; Pelagibacter.
OX   NCBI_TaxID=1977864 {ECO:0000313|EMBL:ARJ47730.1, ECO:0000313|Proteomes:UP000198240};
RN   [1] {ECO:0000313|EMBL:ARJ47730.1, ECO:0000313|Proteomes:UP000198240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS39 {ECO:0000313|EMBL:ARJ47730.1,
RC   ECO:0000313|Proteomes:UP000198240};
RA   Jimenez-Infante F., Ngugi D.K., Stingl U.;
RT   "Genomic Characterization of Two Novel SAR11 Isolates From the Red Sea,
RT   Including the First Strain of the SAR11 Ib clade.";
RL   Submitted (APR-2017) 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; CP020777; ARJ47730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6BCW5; -.
DR   STRING; 1977864.B5L73_02760; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000198240; Chromosome.
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   CDD; cd02013; TPP_Xsc_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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:ARJ47730.1}.
FT   DOMAIN          4..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          188..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..556
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   594 AA;  64891 MW;  B21B9FC54294ACDE CRC64;
     MTKMTTEEAF VKVLQMHGIE HAFGIIGSAF MPISDIFPDA GITFWDVAHE TNGGLIADGY
     TRSTGKMSMV IAQNGPGITG LVTPIKTAYW NHTPLLLVTP QAANKTMGQG GFQEVEQMNL
     FKDMVCYQEE VRDPSRMAEV LNRVIEKAIR GSAPAQINVP RDYWTQVIDI ELPPIVRLER
     QGGGAEAIDK AAKLLSNAKF PVILSGAGVV IGGAIDETKK LAEKLDSPVC SGYQHNDSFP
     GSHPLAVGPL GYNGSKAAME LISKADVVLA LGTRLNPFST LPGYGIDYWP KKASIIQVDI
     NPDRIGLTKK VTVGISGDAK LVAQQIFNKL SSNAGDTDRQ KRKDLIHQTK SAWLQKLSSL
     DHEDDDEGTV WNKEARERDK DRMSPRQAWR AIQAGMPEDV IISSDIGNNC AIGNAYPTFE
     KPRKYLAPGL FGPCGYGFPS ILGAKIGCPD TPVIGFAGDG AFGISMNEMS SCAREEWPAI
     TMVIFRNYQW GAEKRNTTLW FDNNFVGTEL DPELSYAKVA DACGLKGITV KTMEETTAAI
     KQSCEDQKKG ITTFIEVILN QELGEPFRRD AMKKPVRVAG IKKEDMKKQP SLIS
//