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Database: UniProt
Entry: A0A1V0PS51_9RHOB
LinkDB: A0A1V0PS51_9RHOB
Original site: A0A1V0PS51_9RHOB 
ID   A0A1V0PS51_9RHOB        Unreviewed;       591 AA.
AC   A0A1V0PS51;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   ORFNames=RGUI_0799 {ECO:0000313|EMBL:ARE38940.1};
OS   Rhodovulum sp. P5.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=1564506 {ECO:0000313|EMBL:ARE38940.1, ECO:0000313|Proteomes:UP000191808};
RN   [1] {ECO:0000313|EMBL:ARE38940.1, ECO:0000313|Proteomes:UP000191808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P5 {ECO:0000313|EMBL:ARE38940.1,
RC   ECO:0000313|Proteomes:UP000191808};
RA   Tang K.;
RT   "Shallow-sea hydrothermal system.";
RL   Submitted (APR-2016) 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; CP015039; ARE38940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0PS51; -.
DR   STRING; 1564506.RGUI_0799; -.
DR   KEGG; rhc:RGUI_0799; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000191808; Chromosome.
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   ECO:0000313|EMBL:ARE38940.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191808};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ARE38940.1}.
FT   DOMAIN          3..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..555
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   591 AA;  63404 MW;  6EE15D995A0AA740 CRC64;
     MKMTTEEAFV KVLQRHGISD AFGIIGSAFM PISDLFPKAG IRFWDCGHEG SGGMMADGYT
     RASGKVSMMI AQNGPGITNF VTAVKTAYWN HTPLLLVTPQ AANKTMGQGG FQEVEQMKLF
     EDMVAYQEEL RDPSRVAEVL NRVILKAKRA SAPAQINMPR DFWTQVIDID LPAIVEFERP
     AGGAEAIAEA AKLLSEARFP VILNGAGVVI GGAIEASKAL AERLDAPVCC GYQHNDAFPG
     SHPLFAGPLG YNGSKAAMEL IAQADVVLAL GTRLNPFSTL PGYGMDYWPR EARIIQVDIN
     PDRIGLTKPV TVGIVGDAKQ VAGALLAQLS DSAGDAGREE RRATIAQTKS AWAQQLSSMD
     HEEDDPGTTW NERARAAKPD WMSPRMAWRA IQSALPPEAI ISSDIGNNCA IGNAYPSFED
     GRKYLAPGLF GPCGYGLPAI VGAKIACPDT PVVGFAGDGA FGIAVTELTA IGRPEWPAIT
     MVVFRNYQWG AEKRNSTLWY DDNFVGTELG ENVSYAGIAQ ACGLHGIQAF TMEGLTAALK
     KALNDQTEGQ TTLIEAMINQ ELGDPFRRDA MKKPVVVAGI DPADMRPQEP A
//
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