GenomeNet

Database: UniProt
Entry: A0A0P1IV76_9RHOB
LinkDB: A0A0P1IV76_9RHOB
Original site: A0A0P1IV76_9RHOB 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system