ID A0A0T5NWZ9_9RHOB Unreviewed; 592 AA.
AC A0A0T5NWZ9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN ORFNames=XM53_06205 {ECO:0000313|EMBL:KRS13453.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS13453.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS13453.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS13453.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-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:KRS13453.1}.
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DR EMBL; LAXJ01000005; KRS13453.1; -; Genomic_DNA.
DR RefSeq; WP_057791413.1; NZ_LAXJ01000005.1.
DR AlphaFoldDB; A0A0T5NWZ9; -.
DR STRING; 1641875.XM53_06205; -.
DR PATRIC; fig|1641875.4.peg.3604; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051295; 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:SF169; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRS13453.1}.
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"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 63885 MW; DA8B33E7D77DCE0A CRC64;
MKMTTEEAFV KTLQRHGIQH AFGIIGSAMM PISDLFPKAG ITFWDCAHEG SAGMMADGYT
RATGKMSMMI AQNGPGITNF VTAVKTAYWN HTPLLLVTPQ AANKTIGQGG FQEVEQMKLF
EDMVAYQEEV RDPTRVAEVL ARVISQAKRL CGPAQINIPR DFWTQVVDIE IPQAIEFEVS
PGGTKSVAEA AALLSEAKNP VILNGAGVVL SKGGIEASME LAERLTAPVC VGYQHNDAFP
GSHPLFAGPL GYNGSKAGME LIKEADVVLC LGTRLNPFST LPGYGMEYWP ANAKIIQVDI
NPNRIGLTKK VTVGIVGDAA KVAQGILKNL SETAGDHERD ARKAKIAETK SKWAQQLASM
DHEDDDPGTT WNERARDAKP DWMSPRMAWR AIQGALPRNA IISSDIGNNC AIGNAYPDFD
EGRKYLAPGL FGPCGYGLPA IVGAKIGCPD VPVVGFAGDG AFGIAVNELT AIGRSEWPGI
TQIVFRNYQW GAEKRNSTLW FDDNFVGTEL DDDVSYAGIA QACGLKGVVA RTMDELTDAL
NTAIKEQMEN GTTTLIEAMI NQELGEPFRR DAMKKPVEVA GISADDMVEQ RV
//