ID   A0A1Z8VE08_9PROT        Unreviewed;       592 AA.
AC   A0A1Z8VE08;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   ORFNames=CBC21_05490 {ECO:0000313|EMBL:OUU57487.1};
OS   Proteobacteria bacterium TMED61.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1986601 {ECO:0000313|EMBL:OUU57487.1, ECO:0000313|Proteomes:UP000196561};
RN   [1] {ECO:0000313|EMBL:OUU57487.1, ECO:0000313|Proteomes:UP000196561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED61 {ECO:0000313|EMBL:OUU57487.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) 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   -!- 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:OUU57487.1}.
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DR   EMBL; NHDO01000041; OUU57487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z8VE08; -.
DR   Proteomes; UP000196561; 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   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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:OUU57487.1}.
FT   DOMAIN          3..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..557
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          358..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  63725 MW;  F8597729E9832FB8 CRC64;
     MKMTTEEAFI KVLQMHGIEH AFGIIGSAMM PISDLFPAAG IKFWDCAHEC NAGMSADGYT
     RASGKMSMAI AQNGPGITNF VTPVMTAYWN HTPLLLVTPQ AANKTIGQGG FQEVKQMAIF
     QDLVCYQEEV RDPTRIAEVL NRVIEKAHRG SAPAQINVPR DFWTQVIDIE LPQVIGIERS
     PGGADSIARA AALLSEAQFP VILNGAGVVL SGAIEASAAL AEKLSAPVCC NYQHNDAFPG
     SHALSAGPLG YNGSKAAMEL IAQADVVLAL GTRLNPFSTL PGYGTDYWPK EARLIQVDIN
     ADRIGLTKRV EVAIQGDAKR VAEQLLEQLA SQAGDAGRDA RLAEIARSKH AWTEELATMN
     HEDDDPGTTW NQRSRDSQPE RMSPRQAWQA IMAALPKEAI ISSDIGNNCA IGNAYPSFEE
     GRKYLAPGLF GPCGYGFPSI LGAKIGCPDT PVVGFAGDGA FGISMNEMTA CGRNEWPPIT
     MIIFRNYQWG AEKRNTTLWY EDNFVGTELN VGVEYAEVAK ACGVNGVKVE TADALSQALN
     TAIDGQMNNK VTTFIEVVLN QELGEPFRRD AMKAPVAVAG INLSDMCAQQ VN
//