SUFS_DICD3
ID SUFS_DICD3 Reviewed; 412 AA.
AC Q9EXP2; E0SGT8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cysteine desulfurase;
DE EC=2.8.1.7;
DE AltName: Full=Selenocysteine beta-lyase;
DE Short=SCL;
DE AltName: Full=Selenocysteine lyase;
DE EC=4.4.1.16;
DE AltName: Full=Selenocysteine reductase;
GN Name=sufS; OrderedLocusNames=Dda3937_03665;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=11251816; DOI=10.1046/j.1365-2958.2001.02288.x;
RA Nachin L., El Hassouni M., Loiseau L., Expert D., Barras F.;
RT "SoxR-dependent response to oxidative stress and virulence of Erwinia
RT chrysanthemi: the key role of SufC, an orphan ABC ATPase.";
RL Mol. Microbiol. 39:960-972(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [3]
RP FUNCTION, PROBABLE ACTIVE SITE, SUBCELLULAR LOCATION, INTERACTION WITH
RP SUFE, AND MUTAGENESIS OF CYS-369.
RC STRAIN=3937;
RX PubMed=12876288; DOI=10.1074/jbc.m305953200;
RA Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.;
RT "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form
RT a new type of cysteine desulfurase.";
RL J. Biol. Chem. 278:38352-38359(2003).
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:0000269|PubMed:12876288}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
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 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9EXP2; Q9EXP1: sufE; NbExp=3; IntAct=EBI-2121573, EBI-2121567;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12876288}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR EMBL; AJ301654; CAC17128.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98916.1; -; Genomic_DNA.
DR RefSeq; WP_013318359.1; NC_014500.1.
DR AlphaFoldDB; Q9EXP2; -.
DR SMR; Q9EXP2; -.
DR IntAct; Q9EXP2; 1.
DR STRING; 198628.Dda3937_03665; -.
DR EnsemblBacteria; ADM98916; ADM98916; Dda3937_03665.
DR GeneID; 9734155; -.
DR KEGG; ddd:Dda3937_03665; -.
DR PATRIC; fig|198628.6.peg.2706; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_6; -.
DR OMA; HKLCGPT; -.
DR OrthoDB; 446447at2; -.
DR BioCyc; DDAD198628:DDA3937_RS12760-MON; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000006859; 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 1: Evidence at protein level;
KW Cytoplasm; Lyase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..412
FT /note="Cysteine desulfurase"
FT /id="PRO_0000150332"
FT ACT_SITE 369
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000305|PubMed:12876288"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 369
FT /note="C->S: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:12876288"
SQ SEQUENCE 412 AA; 44785 MW; 422BFC09D104DD31 CRC64;
MNYPVEHYPI DRVRADFPIL QQSVNGQPLA YLDSAASAQK PLAVIDRERD FYLHEYAAVH
RGIHTLSARA TSAMEEVRAK VATFIHAASA EDIVFVRGTT EAINLVANSY GRTAFQPGDN
LVISEMEHHA NIVPWQMLAQ ARGLTLRVLP ITDDGELDMA QLPALLDERT RLVAVTQVSN
VLGTVNPLAE IIRQAHACGA KVLVDGAQAV MHQAVDVQAL DCDFYAFSGH KLYGPSGIGV
LYGKSELLQA MPPWEGGGAM IREVSLTQGT TYADPPWRFE AGSPHVAGII GLGAALDYVS
ALGVDAIQAH EGLLMRYALA SLAEVPTLRL YGPVHRQGVI AFNLGRHHAF DVGSFLDQYG
IAIRTGHHCA MPLMSRYGVP SMCRASLALY SCQDEIDRLV AGLHRIHRLL GE
