ID A0A0P1GKA8_9RHOB Unreviewed; 592 AA.
AC A0A0P1GKA8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:CUH76484.1};
GN ORFNames=TRM7557_00922 {ECO:0000313|EMBL:CUH76484.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH76484.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH76484.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH76484.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSD01000014; CUH76484.1; -; Genomic_DNA.
DR RefSeq; WP_058289046.1; NZ_JAQIPA010000020.1.
DR AlphaFoldDB; A0A0P1GKA8; -.
DR STRING; 928856.SAMN04488049_1125; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000052022; 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 ECO:0000313|EMBL:CUH76484.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH76484.1}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 405..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 355..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 63835 MW; 8D7339CE397FD1A3 CRC64;
MRMTTEEAFV KTLQMHGIEH AFGIIGSAMM PISDLFPKAG ITFWDCAHEG SAGMMADGYT
RATGKMSMMI AQNGPGITNF VTAVKTAYWN HTPLLLVTPQ AANKTIGQGG FQEVEQMKLF
EDMVAYQEEV RDPSRVCEVL NRVIMQAKRA SAPAQLNIPR DMWTQVIDVE LPAIVEFERP
SGGETALAEA AALLSDAKNP VILNGAGVVL SKGGIAASKA LAERLDAPVC VGYQHNDAFP
GNHPLFAGPL GYNGSKAGME LIKQADVVLC LGTRLNPFST LPGYGMEYWP ADAKIIQVDI
NPDRIGLTKK VTVGIVGDAA KVATSILSQL ADTAGDEGRE ARKAKIAEEK SRWAQQLASM
DHEDDDPGTT WNQRARADKP DWMSPRMAWR AIQSALPREA IISSDIGNNC AIGNAYPDFD
EGRKYLAPGL FGPCGYGLPA VMGAKIGCPD VPVVGFAGDG AFGIAVNELT AIGRNEWPAV
TQVVFRNYQW GAEKRNSTLW FNDNFVGTEL DQQVSYAGIA NACGLKGVVA RTMDELTSAL
HQAVEDQKNG ITTLIEAMIN QELGEPFRRD AMKQPVAVAG ISAEDMRPQQ VD
//
