ISCS_HELPY
ID ISCS_HELPY Reviewed; 387 AA.
AC O25008;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=HP_0220;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 -!- INTERACTION:
CC O25008; O25852: HP_1262; NbExp=3; IntAct=EBI-7607228, EBI-7731253;
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; AE000511; AAD07288.1; -; Genomic_DNA.
DR PIR; D64547; D64547.
DR RefSeq; NP_207018.1; NC_000915.1.
DR RefSeq; WP_000941691.1; NC_018939.1.
DR PDB; 5WT2; X-ray; 2.30 A; A=1-387.
DR PDB; 5WT4; X-ray; 2.92 A; A=1-387.
DR PDB; 5WT5; X-ray; 1.90 A; A/B/C/D=1-387.
DR PDB; 5WT6; X-ray; 3.30 A; A=1-387.
DR PDB; 6KG0; X-ray; 2.78 A; A=1-387.
DR PDB; 6KG1; X-ray; 2.70 A; A=1-387.
DR PDB; 7CET; X-ray; 2.64 A; A=1-387.
DR PDB; 7CEU; X-ray; 2.90 A; A=1-387.
DR PDBsum; 5WT2; -.
DR PDBsum; 5WT4; -.
DR PDBsum; 5WT5; -.
DR PDBsum; 5WT6; -.
DR PDBsum; 6KG0; -.
DR PDBsum; 6KG1; -.
DR PDBsum; 7CET; -.
DR PDBsum; 7CEU; -.
DR AlphaFoldDB; O25008; -.
DR SMR; O25008; -.
DR DIP; DIP-3630N; -.
DR IntAct; O25008; 5.
DR MINT; O25008; -.
DR STRING; 85962.C694_01110; -.
DR PaxDb; O25008; -.
DR EnsemblBacteria; AAD07288; AAD07288; HP_0220.
DR KEGG; hpy:HP_0220; -.
DR PATRIC; fig|85962.47.peg.238; -.
DR eggNOG; COG1104; Bacteria.
DR OMA; APHIINF; -.
DR PhylomeDB; O25008; -.
DR BRENDA; 2.8.1.7; 2604.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000000429; 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:0006534; P:cysteine metabolic process; IEA:InterPro.
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; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR017773; Cys_deSase_NifS_proteobacteria.
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; TIGR03403; nifS_epsilon; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="Cysteine desulfurase IscS"
FT /id="PRO_0000150269"
FT ACT_SITE 328
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT BINDING 73..74
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 241
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"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6KG0"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5WT5"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5WT5"
FT TURN 182..187
FT /evidence="ECO:0007829|PDB:5WT5"
FT TURN 192..196
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5WT2"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5WT5"
FT TURN 233..237
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:7CET"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:5WT5"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:5WT5"
FT HELIX 363..384
FT /evidence="ECO:0007829|PDB:5WT5"
SQ SEQUENCE 387 AA; 42404 MW; 93AF9C7FB6FC8D94 CRC64;
MLQRIYLDNN ATTRIDPKVK EIMDPFLRDH YGNPSSLHQF GTETHPAIAE ALDKLYKGIN
ARDIDDVIIT SCATESNNWV LKGVYFDECL KKGKNHIVTT VAEHPAVRST CNFLESLGVE
VTYLPINEHG SITAEQVKEA ITEKTALVSV MWANNETGLI FPIEEIGAIC KEKGVLFHTD
AVQAIGKIPV DVLKANADFL SFSAHKFHGP KGIGGLYIRS GVGLTPLFHG GEHMNGRRSG
TLNVPYIVGM GEAMKLAVEH LDYEKEVVGK LRDKLEEALL KIPDVMVVGD RIHRVPNTTL
VSVRGIEGEA MLWDLNRSNI AASTGSACAS EDLEANPVMV AIGASKELAH TAIRLSLSRF
NTEAEIDKTI EVFSQAAVRL RNISSSY
