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Database: UniProt
Entry: A0A0T5P9N6_9RHOB
LinkDB: A0A0T5P9N6_9RHOB
Original site: A0A0T5P9N6_9RHOB 
ID   A0A0T5P9N6_9RHOB        Unreviewed;       562 AA.
AC   A0A0T5P9N6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Sulfoacetaldehyde acetyltransferase {ECO:0000313|EMBL:KRS17891.1};
DE            EC=2.3.3.15 {ECO:0000313|EMBL:QEW27299.1};
GN   Name=xsc_2 {ECO:0000313|EMBL:QEW27299.1};
GN   ORFNames=RIdsm_03111 {ECO:0000313|EMBL:QEW27299.1}, XM52_10025
GN   {ECO:0000313|EMBL:KRS17891.1};
OS   Roseovarius indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS17891.1, ECO:0000313|Proteomes:UP000051401};
RN   [1] {ECO:0000313|EMBL:KRS17891.1, ECO:0000313|Proteomes:UP000051401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B108 {ECO:0000313|EMBL:KRS17891.1,
RC   ECO:0000313|Proteomes:UP000051401};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius indicus B108T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEW27299.1, ECO:0000313|Proteomes:UP000325785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW27299.1,
RC   ECO:0000313|Proteomes:UP000325785};
RA   Vollmers J., Petersen J.;
RT   "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT   geographic distances.";
RL   Submitted (AUG-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}.
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DR   EMBL; LAXI01000005; KRS17891.1; -; Genomic_DNA.
DR   EMBL; CP031598; QEW27299.1; -; Genomic_DNA.
DR   RefSeq; WP_057815842.1; NZ_LAXI01000005.1.
DR   AlphaFoldDB; A0A0T5P9N6; -.
DR   STRING; 540747.SAMN04488031_101234; -.
DR   KEGG; rid:RIdsm_03111; -.
DR   PATRIC; fig|540747.5.peg.4930; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051401; Unassembled WGS sequence.
DR   Proteomes; UP000325785; Chromosome.
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   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; 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   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:0000313|EMBL:QEW27299.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051401};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRS17891.1}.
FT   DOMAIN          4..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          195..330
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          395..541
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   562 AA;  59308 MW;  7EB88881A754A5D0 CRC64;
     MEKMTGGQAA VKALEAEGVS TLFGLIGSAT MEMFDALYDA RGIRFIGVHD ERTGTHMADG
     YARMSGQAGV ILAGQNGPGA TNLVTGLAQA KAAYSPVVSL AGALASGHVY RDAFQEVDQQ
     ALFKPVTKKV WTATGADRVP EMMREAFREA LAPRRGPVQL NLPRDVLSGQ AEFGAFQTPG
     QYRPFAAPAG APEAIDRAAA MLAKAARPVI IAGGGIKNTG AAEPCLALAE AAGCPVVTSP
     GHGDAVPFGH PLNAGQMGPR GNVVASRLVK EADVILALGT RIGFNSTFYS YDNINERAEI
     IQVEMEPTAI GRYFPVSLGI HGDAPTVAGQ LTAALAKMDA RTKAEAWTEA FKAERSAYLQ
     TRDAEADVDS TPLQPSGLFK TLRDVLPKDA AITMDAGTLC LQATDALNYW QPKSLFTPLD
     FGLVGFSFAC GLGVKLAAPD RPVVSLMGDG GFGMTVSELS TAVDHGINTV TVVMNNCCWG
     AEKAYQRDFF GERYIGADVS SPPFDKLAEL YGAKGYRADT LPQLAEAVED ALQCGKPAVI
     DTMVDPSALY SFRRDSFKHR GG
//
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