ISCS2_ARCFU
ID ISCS2_ARCFU Reviewed; 382 AA.
AC O29689;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cysteine desulfurase IscS 2 {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000303|PubMed:22511353};
DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331};
GN Name=iscS2 {ECO:0000255|HAMAP-Rule:MF_00331}; OrderedLocusNames=AF_0564;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S)
RP UNDER REDUCING AND OXIDIZING CONDITIONS AND PYRIDOXAL PHOSPHATE, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=22511353; DOI=10.1002/anie.201201708;
RA Marinoni E.N., de Oliveira J.S., Nicolet Y., Raulfs E.C., Amara P.,
RA Dean D.R., Fontecilla-Camps J.C.;
RT "(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and
RT transfer.";
RL Angew. Chem. Int. Ed. 51:5439-5442(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP ANALOG, FUNCTION, COFACTOR, PROBABLE ACTIVE SITE, MUTAGENESIS OF CYS-321,
RP AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=23160436; DOI=10.1039/c2dt32101g;
RA Yamanaka Y., Zeppieri L., Nicolet Y., Marinoni E.N., de Oliveira J.S.,
RA Odaka M., Dean D.R., Fontecilla-Camps J.C.;
RT "Crystal structure and functional studies of an unusual L-cysteine
RT desulfurase from Archaeoglobus fulgidus.";
RL Dalton Trans. 42:3092-3099(2013).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC produce alanine (Probable). Binds 1 2Fe-2S cluster per subunit in a
CC crystal formed under reducing conditions; this subunit provides 1
CC ligand while IscU provides the other 3 ligands. It is likely that Fe-S
CC cluster coordination is flexible as the role of this complex is to
CC build and then hand off Fe-S clusters. {ECO:0000269|PubMed:22511353,
CC ECO:0000269|PubMed:23160436}.
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 ECO:0000269|PubMed:22511353, ECO:0000269|PubMed:23160436};
CC Note=Cofactor affinity is increased in an IscS-IscU complex.
CC {ECO:0000269|PubMed:22511353, ECO:0000269|PubMed:23160436};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00331}.
CC -!- SUBUNIT: Forms a heterotetramer with IscU, interacts with other sulfur
CC acceptors. {ECO:0000255|HAMAP-Rule:MF_00331,
CC ECO:0000269|PubMed:22511353, ECO:0000269|PubMed:23160436}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
CC -!- MISCELLANEOUS: In Archaea the pyridoxal phosphate cofactor is not
CC covalently bound to Lys but ligated by other amino acids.
CC {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; AE000782; AAB90671.1; -; Genomic_DNA.
DR PIR; D69320; D69320.
DR RefSeq; WP_010878069.1; NC_000917.1.
DR PDB; 4EB5; X-ray; 2.53 A; A/B=1-382.
DR PDB; 4EB7; X-ray; 2.75 A; A/B=1-382.
DR PDB; 4HVK; X-ray; 1.43 A; A=1-382.
DR PDB; 4R5F; X-ray; 1.90 A; A=1-382.
DR PDBsum; 4EB5; -.
DR PDBsum; 4EB7; -.
DR PDBsum; 4HVK; -.
DR PDBsum; 4R5F; -.
DR AlphaFoldDB; O29689; -.
DR SMR; O29689; -.
DR STRING; 224325.AF_0564; -.
DR EnsemblBacteria; AAB90671; AAB90671; AF_0564.
DR GeneID; 1483780; -.
DR KEGG; afu:AF_0564; -.
DR eggNOG; arCOG00066; Archaea.
DR HOGENOM; CLU_003433_0_0_2; -.
DR OMA; FPSEYEY; -.
DR OrthoDB; 25049at2157; -.
DR PhylomeDB; O29689; -.
DR BRENDA; 2.8.1.7; 414.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000002199; 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; 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.
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..382
FT /note="Cysteine desulfurase IscS 2"
FT /id="PRO_0000150288"
FT ACT_SITE 321
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000305|PubMed:23160436"
FT BINDING 70
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:22511353, ECO:0000269|PubMed:23160436"
FT BINDING 149
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:22511353, ECO:0000269|PubMed:23160436"
FT BINDING 234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:22511353"
FT BINDING 321
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 ECO:0000269|PubMed:22511353"
FT MUTAGEN 321
FT /note="C->S: No iron-sulfur cluster assembly."
FT /evidence="ECO:0000269|PubMed:23160436"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 36..55
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4HVK"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:4HVK"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 237..272
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4EB5"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4EB5"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:4HVK"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:4HVK"
FT HELIX 356..375
FT /evidence="ECO:0007829|PDB:4HVK"
SQ SEQUENCE 382 AA; 41824 MW; 3B2A25229124C02A CRC64;
MAYFDYTSAK PVDERVLEAM LPYMTESFGN PSSVHSYGFK AREAVQEARE KVAKLVNGGG
GTVVFTSGAT EANNLAIIGY AMRNARKGKH ILVSAVEHMS VINPAKFLQK QGFEVEYIPV
GKYGEVDVSF IDQKLRDDTI LVSVQHANNE IGTIQPVEEI SEVLAGKAAL HIDATASVGQ
IEVDVEKIGA DMLTISSNDI YGPKGVGALW IRKEAKLQPV ILGGGQENGL RSGSENVPSI
VGFGKAAEIT AMEWREEAER LRRLRDRIID NVLKIEESYL NGHPEKRLPN NVNVRFSYIE
GESIVLSLDM AGIQASTGSA CSSKTLQPSH VLMACGLKHE EAHGTLLLTL GRYNTDEDVD
RLLEVLPGVI ERLRSMSPLY RR
