XSC_ALCXX
ID XSC_ALCXX Reviewed; 603 AA.
AC Q84H41;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Sulfoacetaldehyde acetyltransferase;
DE EC=2.3.3.15;
GN Name=xsc;
OS Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=85698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=NCIMB 10751;
RX PubMed=12358600; DOI=10.1042/bj20021455;
RA Ruff J., Denger K., Cook A.M.;
RT "Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification
RT from Alcaligenes defragrans and gene clusters in taurine degradation.";
RL Biochem. J. 369:275-285(2003).
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 -!- 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 -!- SUBUNIT: Homodimer or homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AY134844; AAN08492.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84H41; -.
DR SMR; Q84H41; -.
DR UniPathway; UPA00336; UER00544.
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 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-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR03457; sulphoacet_xsc; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Direct protein sequencing; Magnesium;
KW Metal-binding; Thiamine pyrophosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..603
FT /note="Sulfoacetaldehyde acetyltransferase"
FT /id="PRO_0000090844"
SQ SEQUENCE 603 AA; 65307 MW; 28D02FB4025A0DC3 CRC64;
MAATDNRKVV EGVHKMTPSE AFVETCVANG VSEMFGIMGS AFMDAMDIFA PAGIRLIPVV
HEQGAAHMAD GYARVSGRHG VVIGQNGPGI SNCVTGIAAA YWAHSPVVIV TPETGTMGMG
LGGFQEANQL PMFQEFTKYQ GHVCNPKRMA EFTGRVFDRA MSEMGPTQLN IPRDYFYGEI
ECEIPKPMRV DRGHGGEASL QAAVELLKTA KFPVILAGGG VVMGDAVEEA KQLAERLGAP
VATGYLRNDA FPAKHPLWAG PLGYQGSKAA MKLIAQADVV IALGSRMGPF GTLPQHGMDY
WPKAAKIIQI EADHTNLGLV KKIAVGINGD AKAVAAELSR RLADVTLGCD ATKAARADTI
ATEKAAWEKE LDGWTHERDP YSLDMIEEAK GERTPTGGSY LHPRQVLREL EKAMPARVMV
STDIGNINSV ANSYLRFDEP RSFFAPMSFG NCGYALPTII GAKCAAPDRP AIAYAGDGAW
GMSMMEIMTA VRHDIPVTAV VFHNRQWGAE KKNQVDFYNR RFVAGELESE SFSDIAKAMG
AEGIVVDHIE DVGPALQKAI DMQMKEGKTC VIEIMCTREL GDPFRRDALS KPVRMLDKYK
DYV
