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Database: UniProt
Entry: A0A0T5NWZ9_9RHOB
LinkDB: A0A0T5NWZ9_9RHOB
Original site: A0A0T5NWZ9_9RHOB 
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
//
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