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Database: UniProt
Entry: A0A0M7BFC7_9RHOB
LinkDB: A0A0M7BFC7_9RHOB
Original site: A0A0M7BFC7_9RHOB 
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}.
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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
//
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