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Database: UniProt
Entry: Q28NE9_JANSC
LinkDB: Q28NE9_JANSC
Original site: Q28NE9_JANSC 
ID   Q28NE9_JANSC            Unreviewed;       593 AA.
AC   Q28NE9;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   OrderedLocusNames=Jann_2846 {ECO:0000313|EMBL:ABD55763.1};
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD55763.1, ECO:0000313|Proteomes:UP000008326};
RN   [1] {ECO:0000313|Proteomes:UP000008326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABD55763.1, ECO:0000313|Proteomes:UP000008326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1 {ECO:0000313|EMBL:ABD55763.1,
RC   ECO:0000313|Proteomes:UP000008326};
RX   PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA   Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA   Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA   Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA   Saunders E., Buchan A.;
RT   "Ecological genomics of marine Roseobacters.";
RL   Appl. Environ. Microbiol. 73:4559-4569(2007).
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; CP000264; ABD55763.1; -; Genomic_DNA.
DR   RefSeq; WP_011455967.1; NC_007802.1.
DR   AlphaFoldDB; Q28NE9; -.
DR   STRING; 290400.Jann_2846; -.
DR   KEGG; jan:Jann_2846; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000008326; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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:ABD55763.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008326};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABD55763.1}.
FT   DOMAIN          3..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..323
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..549
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   593 AA;  63529 MW;  0187D06B412E84F2 CRC64;
     MKMTTEEAFV KTLQMHGIDN AFGIIGSAMM PISDIFPDAG IKFWDCAHEG SAGMMSDGYT
     RATGKISMMI AQNGPGITNF VTAVKTAYWN HTPLLLVTPQ AANKTIGQGG FQEVEQMKLF
     EDMVAYQEEV RDPTRVAEVL TRVISQAKRL SGPAQINIPR DFWTQVVDIE IPEPIEFEAS
     PGGENSVAEA AALLSQAKNP VILNGAGVVL SKGGIDASQA LAERLTAPVC VGYQHNDAFP
     GNHPLFAGPL GYNGSKAGME LIKDADVVLC LGTRLNPFST LPGYGIEYWP ADAKIIQVDI
     NPDRIGLTKK VTVGIVGDAA KVANGILNQL AEDAGDAGRE DRKNHIAQTK SAWAQELSSM
     TEEADDPGTN WNERARAAKP NWMAPRMAWR AIQAALPVEA IISSDIGNNC AIGNAYPSFN
     EGRKYLAPGL FGPCGYGLPA IVGAKIGQPD VPVVGFAGDG AFGIAVNELT AIGRGDWPAI
     TQIVFRNYQW GAEKRNSTLW FDDNFVGTEL DEDVSYSGIA NACGLKGVVA RTQEELTAAL
     DQAIKDQMEN GITTLIEAMI NQELGDPFRR DAMKKPVEVA GISASDMKPQ KVA
//
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