SUFS_ECOL5
ID SUFS_ECOL5 Reviewed; 406 AA.
AC Q0THE9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=ECP_1627;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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}.
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; CP000247; ABG69630.1; -; Genomic_DNA.
DR RefSeq; WP_000144584.1; NC_008253.1.
DR AlphaFoldDB; Q0THE9; -.
DR SMR; Q0THE9; -.
DR STRING; 362663.ECP_1627; -.
DR EnsemblBacteria; ABG69630; ABG69630; ECP_1627.
DR KEGG; ecp:ECP_1627; -.
DR HOGENOM; CLU_003433_2_5_6; -.
DR OMA; HKLCGPT; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000009182; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..406
FT /note="Cysteine desulfurase"
FT /id="PRO_1000070423"
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; 44464 MW; 5C7591401EEE060A CRC64;
MTFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG YAAVHRGIHT
LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL VANSWGNSNV RAGDNIIISQ
MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLETLPTL FDEKTRLLAI THVSNVLGTE
NPLAEMITLA HQHGAKVLVD GAQAVMHHPV DVQALDCDFY VFSVHKLYGP TGIGILYVKE
ALLQEMPPWE GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN
NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF LDNYGIAVRT
GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR IHRLLG
