SUFS_KLEP3
ID SUFS_KLEP3 Reviewed; 406 AA.
AC B5XQH2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Cysteine desulfurase {ECO:0000255|HAMAP-Rule:MF_01831};
DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_01831};
DE AltName: Full=Selenocysteine beta-lyase {ECO:0000255|HAMAP-Rule:MF_01831};
DE Short=SCL {ECO:0000255|HAMAP-Rule:MF_01831};
DE AltName: Full=Selenocysteine lyase {ECO:0000255|HAMAP-Rule:MF_01831};
DE EC=4.4.1.16 {ECO:0000255|HAMAP-Rule:MF_01831};
DE AltName: Full=Selenocysteine reductase {ECO:0000255|HAMAP-Rule:MF_01831};
GN Name=sufS {ECO:0000255|HAMAP-Rule:MF_01831}; OrderedLocusNames=KPK_2184;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-
CC Rule:MF_01831};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01831};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01831}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01831}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01831}.
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DR EMBL; CP000964; ACI07792.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XQH2; -.
DR SMR; B5XQH2; -.
DR EnsemblBacteria; ACI07792; ACI07792; KPK_2184.
DR KEGG; kpe:KPK_2184; -.
DR HOGENOM; CLU_003433_2_5_6; -.
DR OMA; HKLCGPT; -.
DR OrthoDB; 446447at2; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000001734; 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..406
FT /note="Cysteine desulfurase"
FT /id="PRO_1000188303"
FT ACT_SITE 364
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01831"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01831"
SQ SEQUENCE 406 AA; 43728 MW; 492D83EF5C17D9AA CRC64;
MTFSVERVRA DFPVLNREVN GQPLAYLDSA ASAQKPEAVI GAEAEFYRHG YAAVHRGIHT
LSAEATARME AVRQQAANFL NAGSAEEVVF VRGTTEGINL VANSWGNANV GAGDNIIISE
MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLDVVPGL FDPRTRLLAI TEVSNVLGTE
NPLAALIALA HQHGAKVLVD GAQAVMHHPV DVQALGCDFY VFSGHKLYGP TGIGVLYGRS
ELLQAMAPWE GGGSMIATVS LTEGTTWNRA PWRFEAGTPN TGGIIGLGAA LTYVSQLGLT
QIAEYEQTLM RYALEALRAV PDLILYGPAQ RKGVIAFNLG QHHAYDVGSF LDNYGIAVRT
GHHCAMPLMA RYQVPAMCRA SLAMYNTTEE VDRLVAGLQR IHKLLG
