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Database: UniProt
Entry: B8FA04_DESAL
LinkDB: B8FA04_DESAL
Original site: B8FA04_DESAL 
ID   B8FA04_DESAL            Unreviewed;       576 AA.
AC   B8FA04;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   OrderedLocusNames=Dalk_1400 {ECO:0000313|EMBL:ACL03100.1};
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfatibacillaceae; Desulfatibacillum.
OX   NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL03100.1, ECO:0000313|Proteomes:UP000000739};
RN   [1] {ECO:0000313|EMBL:ACL03100.1, ECO:0000313|Proteomes:UP000000739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01 {ECO:0000313|EMBL:ACL03100.1,
RC   ECO:0000313|Proteomes:UP000000739};
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL03100.1; -; Genomic_DNA.
DR   RefSeq; WP_012610535.1; NC_011768.1.
DR   AlphaFoldDB; B8FA04; -.
DR   KEGG; dal:Dalk_1400; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_7; -.
DR   OMA; DGGFLMG; -.
DR   Proteomes; UP000000739; 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:ACL03100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:ACL03100.1}.
FT   DOMAIN          6..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          190..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..541
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   576 AA;  62464 MW;  F97244C2FD109C4C CRC64;
     MAKVKMTPSE ALVETLVAEG VENIFGIVGS AYMDALDLFP TAGIRFISVA HEQAACHAAD
     GLARVTGKPQ ACIAQNGPGA ANFVSAMTAA YWAHSPVVAI TPEAGTLGIG TGGFQELDQM
     PMFHEQTVYQ VRVNAAQRMA ELSRRAFYMA KTYNGPTQLN IPRDLFYGVC EDEIYTTPDI
     TYGSGPRQSL EEAAKLLAEA KYPVILAGGG VSQADAIAEL KALAEYLTAP VVNSYLHNDT
     FPSSHKLSVG PIGYCGSKAA MRTIAKADVV LALGSRLGPF GTLPQYDMTY WPENAKIIQV
     DVNPAVLGLS KRVELAVLAD CREFAKEVFT LVKAAKPGLE EDKARLEDVA NEKKIWDDEL
     EKWSSSTNKL MHPRRFLWEL SRAVPEGSIV ATDIGNNSSM CNSYFQFSGA RQHISALSWG
     NCGFAYGAAM GAKLGCPDKA VFAFQGDGAY GISGIAEVMT AVRENIPIIA IVANNYEWGA
     EKKNQIDYYD NRFIGANLRE NPNYAQLAED MGGKGYRVEN YDEVGDVVKD AVASGKPCVI
     EGVIQGGEEV LAEPFRRDAL KKAYRMLPKY EHLNVK
//
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