SUFS_YERPY
ID SUFS_YERPY Reviewed; 406 AA.
AC B1JJ48;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=YPK_1851;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA68142.1; -; Genomic_DNA.
DR RefSeq; WP_002211805.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JJ48; -.
DR SMR; B1JJ48; -.
DR EnsemblBacteria; ACA68142; ACA68142; YPK_1851.
DR GeneID; 57976274; -.
DR KEGG; ypy:YPK_1851; -.
DR PATRIC; fig|502800.11.peg.2521; -.
DR OMA; HKLCGPT; -.
DR UniPathway; UPA00266; -.
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_1000188316"
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; 44024 MW; 63F744605B8788BD CRC64;
MNFPIERVRA DFPLLSRQVN GQPLVYLDSA ASAQKPQAVI DKELHFYRDG YAAVHRGIHS
LSAEATQQME AVRTQVADFI HAASAEEIIF VRGTTEAINL VANSYGRHFL AAGDSIIITE
MEHHANIVPW QMLAQDLGVE IRVWPLTATG ELEITALAAL IDDTTRLLAV TQVSNVLGTV
NPIKDIVAQA KAAGLVVLVD GAQAVMHQPV DVQALGCDFY VFSGHKLYGP SGIGILYGKS
ALLQQMPPWE GGGAMIKTVS LTQGTTFADA PWRFEAGSPN TAGIMGLGAA IDYVTELGLL
PIQQYEQSLM HYALAQLSQI KSLTLYGPTE RAGVIAFNLG QHHAYDVGSF LDQYGIAIRT
GHHCAMPLMA FYQVPSMCRA SLALYNTRED VDRLVAGLQR IEKLLG
