ID   A0A158BDX1_9BURK        Unreviewed;       614 AA.
AC   A0A158BDX1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   ORFNames=AWB75_03308 {ECO:0000313|EMBL:SAK68006.1};
OS   Caballeronia catudaia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK68006.1, ECO:0000313|Proteomes:UP000054870};
RN   [1] {ECO:0000313|EMBL:SAK68006.1, ECO:0000313|Proteomes:UP000054870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK68006.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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; FCOF02000013; SAK68006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158BDX1; -.
DR   Proteomes; UP000054870; 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   CDD; cd02013; TPP_Xsc_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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:SAK68006.1}.
FT   DOMAIN          27..141
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          212..348
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          434..585
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  66878 MW;  E012B1E7E6DB13F5 CRC64;
     MSEHDQARPS QTTLAATDAA PSGPQAMTPS EAFVETLAAN GVTEMFGIMG SAFMDAMDIF
     APAGIRLIPV VHEQGAGHMA DGYSRVSGRH GVVIGQNGPG ISNAVTAIAA AYWAHSPVVI
     VTPEAGTMGI GLGGFQEAKQ LPMFQEFTKY QGHVTHPARM AEFTARCFDR AMSEMGPTQL
     NIPRDYFYGQ VKVEIPKPQR LDRGPGGDQS LNEAADLLAQ AKFPVIISGG GVVMSDAIEE
     CKALAERLGA PVVNSYLHND SFPANHPLWC GPLGYQGSKA AMKLLNQADV VIALGSRLGP
     FGTLPQHGLD YWPKEAKVIQ IDADHKMLGL VKKISVGICG DAKATAIALT QRLADRKLDC
     DATKDARAKT IADEKAAWEK ELDDWTHERD PYSLDMIEEQ KNEKPFSGGQ YLHPRQVLRE
     LEKAMPEDVM VSTDIGNINS VANSYLRFNK PRSFFAAMSW GNCGYAFPTI IGAKVAAPHR
     PAVSYAGDGA WGMSLMETMT CVRHNIPVTA VVFHNRQWGA EKKNQVDFYN RRFVAGELDN
     QSFAEIARAM GAEGIVVDKL EDVGPALKKA IDLQMNHGKT TIIEIMCTRE LGDPFRRDAL
     AKPVRMLDKY KDYV
//