ID A0A429X609_9BACI Unreviewed; 592 AA.
AC A0A429X609;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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:RST58730.1};
GN ORFNames=D5F11_015940 {ECO:0000313|EMBL:RST58730.1};
OS Siminovitchia terrae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Siminovitchia.
OX NCBI_TaxID=1914933 {ECO:0000313|EMBL:RST58730.1, ECO:0000313|Proteomes:UP000287296};
RN [1] {ECO:0000313|EMBL:RST58730.1, ECO:0000313|Proteomes:UP000287296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29736 {ECO:0000313|EMBL:RST58730.1,
RC ECO:0000313|Proteomes:UP000287296};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) 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:RST58730.1}.
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DR EMBL; QYTW02000017; RST58730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429X609; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000287296; 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 ECO:0000313|EMBL:RST58730.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:RST58730.1}.
FT DOMAIN 19..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..344
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 592 AA; 64535 MW; FD9D0385376F9F82 CRC64;
MVQQETVKQK IATGQKLKMT PSEAIVETLV QENVKEIYGI VGSAFMDMLD LFPTAGIRFI
PVRHEQSAAH MADAFTRVSG TAGVVIGQNG PGITNMVTSV AAAYQAHTPM VVISPSAGTP
TIGWDGFQEA DQVSIFKSIT KETVRVTHTS RVADCLRTAF RIAYAERGPV LYDIPRDLFY
GELEDQILEP HQYRTDARGS GDPALIQKAV ELLKDAKNPV IISGRGAVDA DGVETVVKIA
EHLSAPAAVS YMHNDGFPAD HPLAVGPIGY MGAKSAMRTL KDADVLLAIG TRLSVFGTLP
CYDIDYFPKN AKIIQIDINP RNIARTHPVE VGIIGDAKAA SEELYNQLLK AQPEPAQNAD
RMAEVAKSKE AWEQELVDLA MEPGSPINPR RALLELTRAL PENTIISTDI GNVSSTANAY
LKFNKTRRHI AALTFGNTGF AYPAAMGAQL AEPDTPVVAI IGDGAWGMSL HEVSTAVEQN
IPVIACVFNN KSWAAEKKNQ VDYYDNRFIG SDIEAPDFAE VARSMGALGY TIDKPEDIAG
VVKEVLEKRK PAVLNIFVDG TQLAPPFRRD ALKMPTRFLD KYKHLDHENW KK
//
