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Database: UniProt
Entry: B9NLW5_9RHOB
LinkDB: B9NLW5_9RHOB
Original site: B9NLW5_9RHOB 
ID   B9NLW5_9RHOB            Unreviewed;       591 AA.
AC   B9NLW5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:EEE39029.1};
GN   ORFNames=RKLH11_2875 {ECO:0000313|EMBL:EEE39029.1};
OS   Rhodobacteraceae bacterium KLH11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE39029.1, ECO:0000313|Proteomes:UP000005135};
RN   [1] {ECO:0000313|Proteomes:UP000005135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX   PubMed=21742885; DOI=10.1128/jb.05556-11;
RA   Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT   "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT   Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL   J. Bacteriol. 193:5011-5012(2011).
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; DS999531; EEE39029.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9NLW5; -.
DR   STRING; 467661.RKLH11_2875; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000005135; 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   ECO:0000313|EMBL:EEE39029.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005135};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEE39029.1}.
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..550
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   591 AA;  63595 MW;  2FF71E05D2241589 CRC64;
     MKMTTEEAFV KTLQMHGIEH AFGIIGSAMM PISDIFEKAG ITFWDCAHEG SGGMMADGYT
     RATGKMSMMI AQNGPGITNF VTAVKTAYWN HTPLLLVTPQ AANKTMGQGG FQEMEQMRMF
     ADCVCYQEEV RDPSRMAEVL SRVIMNAKRA SAPAQINVPR DFFTQVVDIE LPAVVEFELP
     SGGASAVSEA AALLSNAKSP VILNGAGTVL SKGGIEASKA LAERLDAPVC VGYQHNDAFP
     GSHPLFAGPL GYNGSKAGME LIKDADVVLC LGTRLNPFST LPGYGMEYWP TDAKIIQVDI
     NPDRIGLTKK VTVGIVGDAA TVATNILHQL SDTAGDEGRD ARKAKIADTK SRWAQELTSM
     DHEQDDPGTT WNERARAAKP DWLSPRKAWR AIQQALPREA IISSDIGNNC AIGNAYPSFD
     EGRKYLAPGL FGPCGYGLPS VIGAKIGCPD VPVVGFSGDG AFGIAVTELT AIGREEWPAV
     TQVVFRNYQW GAEKRNSTLW FDDNFVGTEL DTKVSYAGIA QACGLKGVVA RTMDELTAAL
     NQAIEDQKNG ITTLIEAMIN QELGEPFRRD AMKKPVEVAG IDANDMRAQQ V
//
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