ID A0A2T6KLL7_9RHOB Unreviewed; 593 AA.
AC A0A2T6KLL7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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 ORFNames=C8N45_102109 {ECO:0000313|EMBL:PUB17099.1};
OS Yoonia sediminilitoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=1286148 {ECO:0000313|EMBL:PUB17099.1, ECO:0000313|Proteomes:UP000244523};
RN [1] {ECO:0000313|EMBL:PUB17099.1, ECO:0000313|Proteomes:UP000244523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29955 {ECO:0000313|EMBL:PUB17099.1,
RC ECO:0000313|Proteomes:UP000244523};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-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:PUB17099.1}.
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DR EMBL; QBUD01000002; PUB17099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6KLL7; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000244523; 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:UP000244523};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PUB17099.1}.
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 405..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 593 AA; 64549 MW; B0171437C8AC8D46 CRC64;
MKMTTEEAFV KVLQMHGIDN AFGIIGSAMM PISDLFPQAG IKFWDCAHET SGGMIADGYT
RASGKMSMAI AQNGPGITNF VTPIKTAYWN HTPLLLVTPQ AANKTIGQGG FQEIEQMKLF
EDMVCYQEEV RDPSRMAEVL NRVIEKAWRG SAPAQINIPR DYWTQVIDID LPQIIRLERP
QGGEQAVKDA AKLLSEAEFP VILNGASVVL SGGIDASAKL AEALDAPVAC NYQHNDAFPG
SHPLGVGPLG YNGSKAAMEI IQKADVVLAL GNRLNPFSTL PGYGIDYWPT NAKIIQVDIN
SDRIGLTKKV DVAIQGDAKR VAEQILDNLA DGAGDKGRKE RKELVALTKS RWAQELSSMD
HEDDADEGID WNERARKAKP DHMAPRQAWR AIMSALPKDA IISSDIGNNC AIGNAYPSFD
QGRKYLAPGL FGPCGYGLPA ILGAKIGCPD VPVVGFAGDG AFGISMNEMT ACGRGDWPAI
TMVIFRNYQW GAEKRNTTLW FKDNFVGTEL NEGVNYAEIA KGCGLKGVQC TGMEELTDAL
NTAVREQMND GVTTFIEVVL NQELGEPFRR DAMKKPVSIA GINRDDMKQQ QFV
//
