ID XSC_RHOCB Reviewed; 590 AA.
AC D5AKX8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Sulfoacetaldehyde acetyltransferase {ECO:0000250|UniProtKB:Q84H44};
DE EC=2.3.3.15 {ECO:0000250|UniProtKB:Q84H44};
GN Name=xsc {ECO:0000303|PubMed:17981966};
GN OrderedLocusNames=RCAP_rcc02238 {ECO:0000312|EMBL:ADE85968.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [2]
RP INDUCTION.
RC STRAIN=B10S;
RX PubMed=17981966; DOI=10.1128/jb.01510-07;
RA Wiethaus J., Schubert B., Pfaender Y., Narberhaus F., Masepohl B.;
RT "The GntR-like regulator TauR activates expression of taurine utilization
RT genes in Rhodobacter capsulatus.";
RL J. Bacteriol. 190:487-493(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl phosphate + H(+) + sulfite = phosphate +
CC sulfoacetaldehyde; Xref=Rhea:RHEA:24204, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58246; EC=2.3.3.15;
CC Evidence={ECO:0000250|UniProtKB:Q84H44};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q84H44};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q84H44};
CC -!- PATHWAY: Organosulfur degradation; taurine degradation via aerobic
CC pathway; acetyl phosphate and sulfite from taurine: step 2/2.
CC {ECO:0000250|UniProtKB:Q84H44}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q84H44}.
CC -!- INDUCTION: Induced by taurine via TauR. {ECO:0000269|PubMed:17981966}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001312; ADE85968.1; -; Genomic_DNA.
DR RefSeq; WP_013067947.1; NC_014034.1.
DR AlphaFoldDB; D5AKX8; -.
DR SMR; D5AKX8; -.
DR STRING; 272942.RCAP_rcc02238; -.
DR GeneID; 31491080; -.
DR KEGG; rcp:RCAP_rcc02238; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00336; UER00544.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..590
FT /note="Sulfoacetaldehyde acetyltransferase"
FT /id="PRO_0000430553"
SQ SEQUENCE 590 AA; 63258 MW; 66CDFDA6E2759F9F CRC64;
MRMTTEEAFV KVLQRHGIDT AFGIIGSAFM PISDLFPRAG IRFFDCAHEG SGGMMADGFT
RASGRMAMII AQNGPGVTNF VTAVKTAYWN HTPMLVVTPQ AANRTIGQGG FQEVEQMALF
RDMVCWQEEL RDPARIAEVL DRVIRKARRA SAPAQINLPR DMFTKIIDIE LPQGVDLPRP
APDAQALDRA AALLSSARFP VILNGAGVVL AEAIPDTVAL AERLEAPVCT GYQHNDAFPG
SHPLFAGPLG YNGSKAAMQL MSQADVVLCL GTRLNPFSTL PGYGIDYWPK AAAVIQVDIN
PDRIGLTRPV TLGIAADAGA VARGILARLG AQAGDQDRAE RAARIATTKS RWAQELASMD
HEEDDPGTSW NERARAAKPG WMSPRMAWRA ITAALPPEAI LSSDIGNNCA IGNAYPSFAA
GRKYLAPGLF GPCGYGLPAI IGAKIACPET PVVGFAGDGA FGISVTELTA IGRADWPAIT
MVVFRNYQWG AEKRNSTLWY DDNFVGTELD LQVSYAGIAQ ACGLQGVVAR TMEELTEALR
KALADQAAGK TTLIEALINQ ELGEPFRRDA MTKPVVVAGI DPADMRPQPR
//
