ISCS_VIBCH
ID ISCS_VIBCH Reviewed; 404 AA.
AC Q9KTY2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=VC_0748;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93913.1; -; Genomic_DNA.
DR PIR; G82285; G82285.
DR RefSeq; NP_230397.1; NC_002505.1.
DR RefSeq; WP_000775253.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KTY2; -.
DR SMR; Q9KTY2; -.
DR STRING; 243277.VC_0748; -.
DR DNASU; 2615757; -.
DR EnsemblBacteria; AAF93913; AAF93913; VC_0748.
DR GeneID; 57739458; -.
DR KEGG; vch:VC_0748; -.
DR PATRIC; fig|243277.26.peg.712; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_2_6; -.
DR OMA; APHIINF; -.
DR BioCyc; VCHO:VC0748-MON; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000000584; Chromosome 1.
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; 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 Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Cysteine desulfurase IscS"
FT /id="PRO_0000150281"
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; 44809 MW; 7816AE8ED656530D CRC64;
MKLPIYLDYS ATCPVDPRVA EKMVQYMTMD GTFGNPASRS HRYGWQAEEA VDTAREQIAA
LLNADPREIV FTSGATESDN LAIKGVAHFY NKQGKHIITS KTEHKAVLDT MRQLEREGFE
VTYLDPESNG LVDLAKLEAA MRDDTILVSI MHVNNEIGVV QDIAAIGELC RSRKVVFHVD
AAQSAGKVAI DVQEMKVDLI SLSAHKAYGP KGIGALYVRR KPRIRLEAQM HGGGHERGFR
SGTLPTHQIV GMGEAFRIAK EELQQDYDHA LKLRNRLLDG IKDMEAVTIN GDLDQRVPHN
LNVSFAFVEG ESLLMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFSFGRF
TTEAEIDYAI ELIRVAVDKL RAMSPLWDMY KDGVDLNTVE WAHH
