ID   T1XFX4_VARPD            Unreviewed;       607 AA.
AC   T1XFX4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:AGU51015.1};
GN   ORFNames=VAPA_1c39370 {ECO:0000313|EMBL:AGU51015.1};
OS   Variovorax paradoxus B4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1246301 {ECO:0000313|EMBL:AGU51015.1, ECO:0000313|Proteomes:UP000016223};
RN   [1] {ECO:0000313|EMBL:AGU51015.1, ECO:0000313|Proteomes:UP000016223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:AGU51015.1,
RC   ECO:0000313|Proteomes:UP000016223};
RA   Schuldes J., Brandt U., Hiessl S., Wuebbeler J.H., Thuermer A.,
RA   Steinbuechel A., Daniel R.;
RT   "Genome sequence of Variovorax paradoxus B4.";
RL   Submitted (OCT-2012) 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; CP003911; AGU51015.1; -; Genomic_DNA.
DR   RefSeq; WP_021008469.1; NC_022247.1.
DR   AlphaFoldDB; T1XFX4; -.
DR   KEGG; vpd:VAPA_1c39370; -.
DR   PATRIC; fig|1246301.3.peg.3978; -.
DR   HOGENOM; CLU_013748_3_1_4; -.
DR   OrthoDB; 2254214at2; -.
DR   Proteomes; UP000016223; Chromosome 1.
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   ECO:0000313|EMBL:AGU51015.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:AGU51015.1}.
FT   DOMAIN          20..135
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          205..342
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          427..578
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   607 AA;  65710 MW;  61767A7D2AEEF900 CRC64;
     MSQKQPAAPT REAVAGVQKM TPSEAFVETM VANGVTDMFG IMGSAFMDAM DIFAPAGIRL
     IPVVHEQGGA HMADGYARVS GRHGVVIGQN GPGISNCVTA IAAAYWAHSP VVMITPETGT
     MGMGLGGFQE ANQLPMFQEF TRYQGHVNNP KRMAEYTARC FDRAISEMGP TQLNIPRDYF
     YGEITTEIPK PMRVERGSGG ENSLNAAVEL LASAKFPVIL SGGGVVMGDA VEECKALAER
     LGAPVANGYL RNDSFPASHP LAAGPLGYQG SKAAMKLIAQ ADVVLALGSR MGPFGTLPQH
     GMDYWPKDAK IIQVEADHTN LGLVKKITVG IHGDAKATAN ELLKRLAGKT LACDATKSQR
     AEKIKAEKAA WEKELDEWTH ERDPFSLDAI EEAKGEKTPT GGSYLHPRQV LRELEKAMPP
     RVMVSTDIGN INAIANSYLR FEEPRSFFAP MSFGNCGYSL PTMIGAKCAA PDRPAVAYAG
     DGAWGMSMVE IMTAVRHDIP VTAVVFHNRQ WGAEKKNQVD FYNRRFVAGE LESESFAGIA
     KAMGAEGIVV DRLEDVGPAL KKAIDMQMNQ GKTCVIEIMC TRELGDPFRR DALAKPVRFL
     EKYKDYV
//