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   27-MAR-2024, entry version 133.
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};
GN   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   PaxDb; 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   OrthoDB; 9577at2157; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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
//