ID A0A1I6Z183_9BURK Unreviewed; 600 AA.
AC A0A1I6Z183;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN ORFNames=SAMN05192563_100284 {ECO:0000313|EMBL:SFT56476.1};
OS Paraburkholderia aspalathi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1324617 {ECO:0000313|EMBL:SFT56476.1, ECO:0000313|Proteomes:UP000198844};
RN [1] {ECO:0000313|EMBL:SFT56476.1, ECO:0000313|Proteomes:UP000198844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27731 {ECO:0000313|EMBL:SFT56476.1,
RC ECO:0000313|Proteomes:UP000198844};
RA de Groot N.N.;
RL Submitted (OCT-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; FPBH01000002; SFT56476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6Z183; -.
DR Proteomes; UP000198844; 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:SFT56476.1}.
FT DOMAIN 13..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 420..571
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 600 AA; 65258 MW; 778713DEAC573298 CRC64;
MSDHTPVSGP QAMTPSEAFV ETLAANGVTD MFGIMGSAFM DAMDIFAPAG IRLIPVVHEQ
GAGHMADGYA RVSGRHGVVI GQNGPGISNC VTAIAAAYWA HSPVVMITPE AGTMGIGLGG
FQEAKQLPMF QEFTKYQGHV THPARMAEFT GRCFDRALAE MGPTQLNIPR DYFYGQIKAE
IPQPQRLDRG PGGDQRLNEA AELLAQAKFP VIISGGGVVM ADAIEECKAL AERLGAPVVN
SYLHNDSFPA DHPLWCGPLG YQGSKAAMKL IQRADVVIAL GSRLGPFGTL PQHGMDYWPQ
NAKIIQIDAD HKMLGLVKKI SVGICGDAKA AAVALAQRLE GRTLVCDASR EERAGEIAAE
KAAWEKELDG WTHERDPYSM DMIEEQKDER TPGGGNYLHP RQVLRELEKA MPDDVMVSTD
IGNINSVANS YLRFKKPRSF FAAMSWGNCG YAFPTIIGAK VAAPHRPAVS YAGDGAWGMS
LMETMTCVRH NIPVTAVVFH NRQWGAEKKN QVDFYNRRFV AGELDNQSFA GIARAMGAEG
VTVDRLEDVG PALKRAIDAQ MNHGKTTIIE IMCTRELGDP FRRDALAKPV RLLDKYKDYV
//