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Database: UniProt
Entry: A0A0K9GVS6_9BACI
LinkDB: A0A0K9GVS6_9BACI
Original site: A0A0K9GVS6_9BACI 
ID   A0A0K9GVS6_9BACI        Unreviewed;       587 AA.
AC   A0A0K9GVS6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   ORFNames=AC625_15395 {ECO:0000313|EMBL:KMY50728.1};
OS   Peribacillus loiseleuriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY50728.1, ECO:0000313|Proteomes:UP000037146};
RN   [1] {ECO:0000313|Proteomes:UP000037146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMY50728.1}.
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DR   EMBL; LFZW01000001; KMY50728.1; -; Genomic_DNA.
DR   RefSeq; WP_049682080.1; NZ_LFZW01000001.1.
DR   AlphaFoldDB; A0A0K9GVS6; -.
DR   STRING; 1679170.AC625_15395; -.
DR   PATRIC; fig|1679170.3.peg.3505; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000037146; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000037146};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:KMY50728.1}.
FT   DOMAIN          14..129
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          201..337
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..551
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   587 AA;  64036 MW;  F4C2F25A6F97C551 CRC64;
     MAETKTLRGT KVKMTPSEAI VETLVAEGVK HISGILGSAF MDMLDLLPTA GIRFIGVRHE
     QSAAHMEDAY CRVSGVAGVV IGQNGPGMTN MVTSVAAANQ AHTPMVVISP SAGTPTVGWD
     GFQECDQVSV FKAITKETVR VTHPGRVADC LRTAFRIAYA ERGPVLFDIP RDYFYGEVED
     QILKPHQYRV DSRGCGSSES LDRAAEILAN AEYPVIISGR GTVDSDGIEE IRNIAEHLTA
     PVAVSYMHND AFPADHPLAV GPIGYMGSKA AMNTLKQADV ILAVGTRLSV FGTLPCYDID
     YFPKDAQIIQ IDINPRQIAR THPVEVGIIG DAREASREIM KRLKDIKPNP KQEKLRLGEI
     THEKQKWEQE LVDLAMIDGT PINPRRALLE LTKVLPENAI VTTDIGNVSS TANAYLKFNR
     SRRHIAALTF GNTGFAYPSA LGAKLAEPNA PVIAIVGDGA WGMSLHEVST AVEENIPVIA
     CVFNNNAWCA EKKNQVDFYN NRFVGADIQN PDFAEVARSM GAVGIRVETP EELGPVIEEA
     IKLNKPTVID IQVDGTQLAP PFRKDALKMP TRLLAKYSHL DHKNWDK
//
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