ID   SUFS_PECAS              Reviewed;         407 AA.
AC   Q6D625;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=ECA1863;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG74766.1; -; Genomic_DNA.
DR   RefSeq; WP_011093433.1; NC_004547.2.
DR   AlphaFoldDB; Q6D625; -.
DR   SMR; Q6D625; -.
DR   STRING; 218491.ECA1863; -.
DR   PRIDE; Q6D625; -.
DR   EnsemblBacteria; CAG74766; CAG74766; ECA1863.
DR   GeneID; 57209430; -.
DR   KEGG; eca:ECA1863; -.
DR   PATRIC; fig|218491.5.peg.1892; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_6; -.
DR   OMA; HKLCGPT; -.
DR   OrthoDB; 446447at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000007966; 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; IPR016454; Cysteine_dSase.
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   PIRSF; PIRSF005572; NifS; 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; Reference proteome; Transferase.
FT   CHAIN           1..407
FT                   /note="Cysteine desulfurase"
FT                   /id="PRO_0000150333"
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   407 AA;  44372 MW;  762DDD5965F00B57 CRC64;
     MSYPIERVRA DFPLLASEVN GQPLAYLDSA ASAQKPHSVI DREAEFYRHE YAAVHRGIHT
     LSAQATSAME AVREKVASFI NAASAEEIVF VRGTTEAINL VANSYGRTFI QPGDNLIITE
     MEHHANIVPW QMLAEAHGVE VRVLPLAEDG SLDVAQLPVL LDERTRLLAV TQISNVLGTL
     NPVKAMIAQA KAAGAVVLID GAQSIMHQPV DVQDLDCDFF VFSGHKIYGP SGIGVLYGKR
     DLLQAMPPWE GGGAMIRQVS LRTGITYADS PWRFEAGSPN TGGIMGLGAA LDYVTALGRE
     DIQRYESSLM QYALEALTQV PDLTLYGPAE RHGVIAFNLG QHHAYDVGSF LDRYGIAIRT
     GHHCAMPLME HYGVPSMCRA SLAVYTTREE IDRLVAGLQR IHRLLGS