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
//