ID C0Q606_SALPC Unreviewed; 449 AA.
AC C0Q606;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|HAMAP-Rule:MF_01831};
DE EC=2.8.1.7 {ECO:0000256|HAMAP-Rule:MF_01831};
DE AltName: Full=Selenocysteine beta-lyase {ECO:0000256|HAMAP-Rule:MF_01831};
DE Short=SCL {ECO:0000256|HAMAP-Rule:MF_01831};
DE AltName: Full=Selenocysteine lyase {ECO:0000256|HAMAP-Rule:MF_01831};
DE EC=4.4.1.16 {ECO:0000256|HAMAP-Rule:MF_01831};
DE AltName: Full=Selenocysteine reductase {ECO:0000256|HAMAP-Rule:MF_01831};
GN Name=sufS {ECO:0000256|HAMAP-Rule:MF_01831,
GN ECO:0000313|EMBL:ACN46472.1};
GN OrderedLocusNames=SPC_2356 {ECO:0000313|EMBL:ACN46472.1};
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN46472.1, ECO:0000313|Proteomes:UP000001599};
RN [1] {ECO:0000313|EMBL:ACN46472.1, ECO:0000313|Proteomes:UP000001599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN46472.1,
RC ECO:0000313|Proteomes:UP000001599};
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to
CC yield L-alanine, an essential step in sulfur metabolism for
CC biosynthesis of a variety of sulfur-containing biomolecules. Component
CC of the suf operon, which is activated and required under specific
CC conditions such as oxidative stress and iron limitation. Acts as a
CC potent selenocysteine lyase in vitro, that mobilizes selenium from L-
CC selenocysteine. Selenocysteine lyase activity is however unsure in
CC vivo. {ECO:0000256|HAMAP-Rule:MF_01831}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC ChEBI:CHEBI:57972; EC=4.4.1.16; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01831};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357, ECO:0000256|HAMAP-
CC Rule:MF_01831};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01831, ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01831}.
CC -!- SUBUNIT: Homodimer. Interacts with SufE and the SufBCD complex composed
CC of SufB, SufC and SufD. The interaction with SufE is required to
CC mediate the direct transfer of the sulfur atom from the S-
CC sulfanylcysteine. {ECO:0000256|HAMAP-Rule:MF_01831}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01831}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC ECO:0000256|HAMAP-Rule:MF_01831}.
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DR EMBL; CP000857; ACN46472.1; -; Genomic_DNA.
DR AlphaFoldDB; C0Q606; -.
DR KEGG; sei:SPC_2356; -.
DR HOGENOM; CLU_003433_2_5_6; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000001599; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009000; F:selenocysteine lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR CDD; cd06453; SufS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01831; SufS_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010970; Cys_dSase_SufS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01979; sufS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01831};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01831, ECO:0000313|EMBL:ACN46472.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01831}; Transferase {ECO:0000256|HAMAP-Rule:MF_01831}.
FT DOMAIN 26..394
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT ACT_SITE 364
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01831"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01831"
SQ SEQUENCE 449 AA; 49754 MW; D5FD5D59EE33BCE9 CRC64;
MTFPVEKVRA DFPILQREVN GLPLAYLDSA ASAQKPNQVI DAESAFYRHG YAAVHRGIHT
LSAQATESME NVRKQASRFI NARSAEELVF VRGTTEGINL VANSWGTENI RAGDNIIISE
MEHHANIVPW QMLCERKGAE LRVIPLHPDG TLRLETLAAL FDDRTRLLAI THVSNVLGTE
NPLPDMIALA RQHGAKVLVD GAQAVMHHVV DVQALDCDFY VFSGHKLYGP TGIGILYVKE
ALLQEMPPWE GGGSMISTVS LTQGTTWAKA PWRFEAGTPN TGGIIGLGAA IDYVTSLGLD
KIGDYEQMLM RYALEQLAQV PDITLYGPAQ RLGVIAFNLG KHHAYDVGSF LDNYGIAVRT
GHHCAMPLMA WYGVPAMCRA SLAMYNTHEE VDRLVAGLTR IHRLLDWDNS EVLWLRYRIK
KNCCVTLRVA LIGKRNIYIL LSWGSAWRS
//
