ID A0A0M2HAE0_9MICO Unreviewed; 554 AA.
AC A0A0M2HAE0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Sulfoacetaldehyde acetyltransferase {ECO:0000313|EMBL:KJL41134.1};
DE EC=2.3.3.15 {ECO:0000313|EMBL:KJL41134.1};
GN Name=xsc {ECO:0000313|EMBL:KJL41134.1};
GN ORFNames=RS82_03050 {ECO:0000313|EMBL:KJL41134.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41134.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL41134.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41134.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL41134.1}.
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DR EMBL; JYJA01000038; KJL41134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2HAE0; -.
DR PATRIC; fig|69370.6.peg.3104; -.
DR Proteomes; UP000034098; Unassembled WGS sequence.
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 CDD; cd00568; TPP_enzymes; 1.
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; 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 PANTHER; PTHR18968:SF13; 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:0000313|EMBL:KJL41134.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KJL41134.1}.
FT DOMAIN 7..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 57040 MW; A76B5EAD477842BE CRC64;
MSPAMSTVSA HVALTLARHI DHVFGVMGNG NAYFLDALKR STDVHFTAVR HEAGGVVAAD
AYHRASGRLA AATATYGAGF TNTITALAEA VQAHVPLVLV VGDEPTSGPR PWDVDQIALA
SAVGARTYTV GRADAAATTI IAIEHALTYR VPTVLAIPYD VAARDAGPLP EAPEPRLPAP
LVPAGPFAEG AVEGLVEALA SAERPFLLAG RGAWISGAGE ALGDVADAVG AITATTALGR
GVFPRGEFDL GVTGGFGAEG AMELVRQADV AVVFGASLNQ FTMRFGELFA PGTRVFQVDV
APAATHPHVG GYVRGDAAVV ARALADGLQA RGGAPSGWRE SVDLMPLRAY EQGHGVAPDG
RLDPRTVAAR IGALLPEDRV VVSDGGHFIG WANMYWPVAS PDRMTMVGTA FQSIGLGWPS
VPGAALAKPS ATVVLTTGDG GGLMALADLE TAVRVAGGRG IAVVWNDAAY GAEINLYGLK
GLAREPMLIP EVDFAALAAG VGAEGVVVRT LADLDRLADW AAEPAASRPF LVLDCRISGE
VIAPYQREII RVNS
//
