ID A0A0P1IV76_9RHOB Unreviewed; 589 AA.
AC A0A0P1IV76;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:CUK27382.1};
GN ORFNames=TA5114_03210 {ECO:0000313|EMBL:CUK27382.1};
OS Cognatishimia activa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK27382.1, ECO:0000313|Proteomes:UP000051184};
RN [1] {ECO:0000313|Proteomes:UP000051184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-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}.
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DR EMBL; CYUE01000022; CUK27382.1; -; Genomic_DNA.
DR RefSeq; WP_058316290.1; NZ_CYUE01000022.1.
DR AlphaFoldDB; A0A0P1IV76; -.
DR STRING; 1715691.TA5113_00609; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051184; 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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:CUK27382.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051184};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CUK27382.1}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 351..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 63602 MW; 5709F7DE22DABEDE CRC64;
MKMTTEEAFV KVLQMHGIDN AFGIIGSAMM PISDLFPAAG IKFFDCAHEC NAGMMADGYT
RATGKMSMMV AQNGPGITSL VTPIKTAYWN HTPLLIVTPQ AANKTIGQGG FQEVEQMALL
EDMVAYQEEV RDPTRMAEVL NRVILQAKRA SAPAQINVPR DFWTQVIDIE LPAVVEFERP
QGGEDAVKKA AELLSNAKFP VILNGAGVVL GDAIGDSAEL AERLTAPVCV GYQHNDAFPG
SHPLFAGPLG YNGSKAGMEL IAKADVVLAL GTRLNPFSTL PGYGIDYWPK DAKIIQVDIN
PDRIGLTKPV TVGIVGDAKK VAQGILSQLS GTAGDEGREA RKNTIADAKS SWAQQLTSMD
HEDDDPGTTW NERARGREPE KMSPRMAWRA IQASLPKDAI ISSDIGNNCA IGNAYPSFED
GRKYLAPGLF GPCGYGFPAI CGAKVGCPDT PVVGFAGDGA FGISMNEMVS VNRDDWPPIT
MIIFRNYQWG AEKRNTTLWF DDNFVGTELS QEVSYAGIAK ACGVHGVAVS TMEDLTGELA
KAVKRQMEDK ETTFIEILLN QELGEPFRRD AMKKPVSVAG ISREDMRAQ
//