(data stored in ACNUC7421 zone)

SWISSPROT: ISCS_HISS2

ID   ISCS_HISS2              Reviewed;         404 AA.
AC   B0UVL5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 72.
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=HSM_0154;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000947; ACA31296.1; -; Genomic_DNA.
DR   RefSeq; WP_012340679.1; NC_010519.1.
DR   SMR; B0UVL5; -.
DR   EnsemblBacteria; ACA31296; ACA31296; HSM_0154.
DR   GeneID; 31486432; -.
DR   KEGG; hsm:HSM_0154; -.
DR   HOGENOM; HOG000017510; -.
DR   KO; K04487; -.
DR   OMA; EPIQSGG; -.
DR   OrthoDB; 839689at2; -.
DR   BioCyc; HSOM228400:G1GB8-159-MONOMER; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000008543; 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   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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; B0UVL5.
DR   SWISS-2DPAGE; B0UVL5.
KW   2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..404
FT                   /note="Cysteine desulfurase IscS"
FT                   /id="PRO_1000079205"
FT   REGION          75..76
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   REGION          203..205
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   ACT_SITE        328
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   METAL           328
FT                   /note="Iron-sulfur (2Fe-2S); via persulfide group; shared
FT                   with IscU"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         155
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         183
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         243
FT                   /note="Pyridoxal phosphate"
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;  45122 MW;  058333265C96C7F4 CRC64;
     MKLPIYLDYA ATCPVDERVV KKMMEFLSID GNFGNPASRS HKFGWQAEEA VDVARNHIAD
     LIGADSREIV FTSGATEADN LALKGVMRFY QTKGKHLITC KTEHKAILDT CRQLEREGFE
     VTYLDPKSDG LIDLEELKSV IRDDTVLVSI MHANNEIGVV QDIAKIGEIC RERKVLFHTD
     ATQSVGKLPI NLSELKVDLL SMSSHKLYGP KGIGALYVCR KPRVRLEAII HGGGHERGMR
     SGTLPVHQIV GMGEAYRIAK EEMATEMPRL TALRDRLYNG LKDIEETYVN GSMEQRLGNN
     LNISFNYVEG ESLMMALRDI AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFTVGRY
     TTEEEIDYSI GLVKSAVKKL RDLSPLWDMF KEGIDLNSIE WTHH
//

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