ID   A0A0P1ILV0_9RHOB        Unreviewed;       592 AA.
AC   A0A0P1ILV0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   Name=xsc_1 {ECO:0000313|EMBL:CUK10756.1};
GN   ORFNames=PH7735_03489 {ECO:0000313|EMBL:CUK10756.1};
OS   Shimia thalassica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUK10756.1, ECO:0000313|Proteomes:UP000051870};
RN   [1] {ECO:0000313|Proteomes:UP000051870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA   Rodrigo-Torres Lidia, Arahal R.David.;
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; CYTW01000005; CUK10756.1; -; Genomic_DNA.
DR   RefSeq; WP_058312661.1; NZ_CYTW01000005.1.
DR   AlphaFoldDB; A0A0P1ILV0; -.
DR   STRING; 1715693.PH7735_03489; -.
DR   GeneID; 83882466; -.
DR   Proteomes; UP000051870; 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; 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   ECO:0000313|EMBL:CUK10756.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051870};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:CUK10756.1}.
FT   DOMAIN          3..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..322
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..556
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          358..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  63933 MW;  D6E67748F464A45F CRC64;
     MKMTTEEAFV KVLQMHGIDH AFGIIGSAMM PISDLFPAAG IKFFDCAHEC NAGMMADGFT
     RASGDMSMMV AQNGPGITSL VTPIKTAYWN HTPLLIVTPQ AANKTMGQGG FQEVEQMALL
     EDMVAYQEEV RDPSRMAEVL NRVILQAKRA SAPAQINIPR DYWTQVIDIE LPAVVEFERP
     AGGEKAVAEA AKLLSEARFP VILNGAGVVL GDAIRDSMAL AERLDAPVCV GYQHNDAFPG
     SHPLFAGPLG YNGSKAGMEL IAKADVVLAL GTRLNPFSTL PGYGIDYWPE NAKIIQVDIN
     PDRIGLTKTV SVGIVGDAKK VANGILAQLG EIAGDTNRAE RKAMISQIKS TWAQELTSMD
     HEDDDPGTTW NARARDREPQ KMSPRKAWRA IQSALPKEAI ISSDIGNNCA IGNAYPAFEQ
     GRKYLAPGLF GPCGYGFPSI CGAKIACPDV PVVGFAGDGA FGISMNEMVS VKRDDWPAIT
     MVIFRNYQWG AEKRNTTLWF DDNFVGTELS QDVSYAGIAR ACGVEGVAVS TMEDLTDALD
     KAIKAQMQDG TTTFIEVLLN QELGEPFRRD AMKKPVSVAG ISAADMRSKR RA
//