ID A0A0C4YMM7_9BURK Unreviewed; 612 AA.
AC A0A0C4YMM7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN ORFNames=RR42_s2701 {ECO:0000313|EMBL:AJG24283.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24283.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG24283.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG24283.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010537; AJG24283.1; -; Genomic_DNA.
DR RefSeq; WP_043356360.1; NZ_CP010537.1.
DR AlphaFoldDB; A0A0C4YMM7; -.
DR STRING; 68895.RR42_s2701; -.
DR KEGG; cbw:RR42_s2701; -.
DR Proteomes; UP000031843; Chromosome secondary.
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: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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:AJG24283.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AJG24283.1}.
FT DOMAIN 25..139
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 210..347
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 432..583
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 66558 MW; 047D7F61E899CDC5 CRC64;
MSEHLPETLA AGTQAGTATT GPQEMTPSEA FVETLAANGV TDMFGIMGSA FMDAMDIFAP
AGIRLIPVVH EQGAGHMADG YARVSGRHGV VIGQNGPGIS NCVTAIAAAY WAHSPVVIVT
PEAGTMGIGL GGFQEAKQLP MFQEFTKYQG HVTHPARMAE YTGRCFDRAM AEMGPTQLNI
PRDYFYGQIK AEIPQPQRLD RGPGGDQRLN EAAELIAKAR FPVIISGGGV VMADAIEQCQ
ALAERLGAPV VNSYLHNDSF PASHPLWCGP LGYQGSKAAM KLLARADVVI ALGSRLGPFG
TLPQHGMDYW PKHAKIIQID ADHKMLGLVK KISVGICGDA KAAAVALTER LAGRTLACDA
SREDRAGQIA AEKAAWEKEL DEWTHERDPY SLDMIEEQKH ERTPTGGHYL HPRQVLRELE
KAMPDDVMVS TDIGNINSVA NSYLRFNKPR SFFAAMSWGN CGYAFPTIMG AKVAAPHRPA
VSYAGDGAWG MSLMETMTAV RHNIPVTAVV FHNRQWGAEK KNQVDFYNRR FVAGELDNQS
FAEIARAMGA EGIVVDKLED VGPALKRAID LQMNHGKTTI IEIMCTRELG DPFRRDALAK
PVRMLDKYKD YV
//