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ISCS_PSEE4
ID   ISCS_PSEE4              Reviewed;         404 AA.
AC   Q1IEJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331};
DE            EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331};
GN   Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331}; OrderedLocusNames=PSEEN1010;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
CC   -!- FUNCTION: Master enzyme that delivers sulfur to a number of partners
CC       involved in Fe-S cluster assembly, tRNA modification or cofactor
CC       biosynthesis. Catalyzes the removal of elemental sulfur atoms from
CC       cysteine to produce alanine. Functions as a sulfur delivery protein for
CC       Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as
CC       well as other S acceptor proteins. {ECO:0000255|HAMAP-Rule:MF_00331}.
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_00331};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00331};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00331}.
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, interacts with
CC       other sulfur acceptors. {ECO:0000255|HAMAP-Rule:MF_00331}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00331}.
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DR   EMBL; CT573326; CAK13913.1; -; Genomic_DNA.
DR   RefSeq; WP_011532336.1; NC_008027.1.
DR   AlphaFoldDB; Q1IEJ2; -.
DR   SMR; Q1IEJ2; -.
DR   STRING; 384676.PSEEN1010; -.
DR   PRIDE; Q1IEJ2; -.
DR   EnsemblBacteria; CAK13913; CAK13913; PSEEN1010.
DR   KEGG; pen:PSEEN1010; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_2_6; -.
DR   OMA; KGLYWAR; -.
DR   OrthoDB; 839689at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010240; Cys_deSase_IscS.
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   PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02006; IscS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..404
FT                   /note="Cysteine desulfurase IscS"
FT                   /id="PRO_1000019424"
FT   ACT_SITE        328
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         75..76
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         155
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         183
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         203..205
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         243
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         328
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared with IscU"
FT                   /note="via persulfide group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
SQ   SEQUENCE   404 AA;  44441 MW;  EA109778AE5A8EFC CRC64;
     MKLPIYLDYS ATTPVDPRVA QKMAECLLVD GNFGNPASRS HVFGWKAEEA VENGRRQVAE
     LINADPREIV WTSGATESDN LALKGVAHFY QTKGKHIITS KIEHKAVLDT ARQLEREGFE
     VTYLEPGEDG IVTPAMVEAA LRDDTILVSL MHVNNEVGSI NDIAAIGELT RSRGVLFHVD
     AAQSAGKVEI DVQKLKVDLM SFSAHKVYGP KGIGALYVSR KPRVRLEAII HGGGHERGMR
     SGTLPTHQIV GMGEAFAIAK QEMAAENVRI KALSDRFFKQ VSDLEELYVN GSQTARVPHN
     LNLSFNYVEG ESLLMSLKDI AVSSGSACTS ASLEPSYVLR ALGRNDELAH SSIRFSFGRF
     TTEEEVDYAA QEVCKAVNKL RELSPLWDMY KDGVDISKIE WAAH
 
 
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