ID A0A0M7BFC7_9RHOB Unreviewed; 590 AA.
AC A0A0M7BFC7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:CUH40889.1};
GN ORFNames=JSE7799_03629 {ECO:0000313|EMBL:CUH40889.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH40889.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH40889.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH40889.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYPR01000240; CUH40889.1; -; Genomic_DNA.
DR RefSeq; WP_055664881.1; NZ_CYPR01000240.1.
DR AlphaFoldDB; A0A0M7BFC7; -.
DR STRING; 313367.JSE7799_03629; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000049455; 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:CUH40889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049455};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH40889.1}.
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..558
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 63576 MW; 470C95BA2A00260A CRC64;
MRMTTEEAFV KVLQRHGIRH AFGIIGSAMM PISDIFPAAG ITFWDAAHEG SAGFMADGYT
RATGEMSMMI AQNGPGITNF VTAVKTAYWN HTPLLLVTPQ AANKTIGQGG FQEVEQMKLF
EDMVAYQEEV RDPSRIAEVL TRVIAKARRL SGPAQINVPR DFWTQEIDVA LPDPVVLEVS
PGGENSVKAA AQLLDGAKNP VILNGAGVVL SEGGIAASMA LAERLGAPVC VGYQHNDAFP
GGHPLFAGPL GYNGSKAAMR LISEADVVLA LGTRLNPFST LPGYGLEYWP ADAKLIQVDI
NPDRIGLTKK VSVGIVGDAA KVARGILADL SDTAGDHGRE ARADRIAQVK SAWAQELSSL
DHEEDDDGTT WNERARADKP DWMSPRMAWR AIQSALPREA IISSDIGNNC AIGNAYPDFD
EGRHYLAPGL FGPCGYGLPS IVGAKIGRPD LPVVGFAGDG AFGIAVTELT AIGRDEWPAI
TQIVFRNYQW GAEKRNSTLW FDDNFVGTEL DTRVSYAGIA QACGLLGVQV RTMEALTDAL
SEAIRTQMQD KRTTLIEVML NQELGEPFRR DAMKKPVRVA GIDRADMAVE
//