ISCS_AZOVI
ID ISCS_AZOVI Reviewed; 404 AA.
AC O31269;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000303|PubMed:9582371};
DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:9582371};
GN Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-23; 3-18; 241-257;
RP 319-340 AND 382-391, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=9582371; DOI=10.1074/jbc.273.21.13264;
RA Zheng L., Cash V.L., Flint D.H., Dean D.R.;
RT "Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx
RT gene cluster from Azotobacter vinelandii.";
RL J. Biol. Chem. 273:13264-13272(1998).
RN [2]
RP FUNCTION, INTERACTION WITH ISCU, SUBUNIT, PATHWAY, AND REACTION MECHANISM.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX DOI=10.1021/ja9944195;
RA Agar J.N., Zheng L., Cash V.L., Dean D.R., Johnson M.K.;
RT "Role of the iscU protein in iron-sulfur cluster biosynthesis: IscS-
RT mediated assembly of a [Fe2S2] cluster in IscU.";
RL J. Am. Chem. Soc. 122:2136-2137(2000).
RN [3]
RP FUNCTION IN FE-S CLUSTER FORMATION, REACTION MECHANISM, AND SUBUNIT.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=10891064; DOI=10.1021/bi000931n;
RA Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., Johnson M.K.;
RT "IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential
RT assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU.";
RL Biochemistry 39:7856-7862(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 from cysteine
CC to produce alanine via an enzyme-bound persulfide intermediate.
CC Functions as a sulfur delivery protein for Fe-S cluster synthesis.
CC Cluster assembly on IscU homodimers proceeds sequentially from 1 2Fe-2S
CC per dimer, to 2 2Fe-2S per dimer and finally 1 4Fe-4S per dimer.
CC {ECO:0000269|PubMed:10891064, ECO:0000269|PubMed:9582371,
CC ECO:0000269|Ref.2}.
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, ECO:0000269|PubMed:9582371};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00331,
CC ECO:0000269|PubMed:9582371};
CC -!- ACTIVITY REGULATION: Inhibited by equimolar N-iodoacetyl-N'-(5-sulfo-1-
CC naphthyl)ethylenediamine. {ECO:0000269|PubMed:9582371}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|Ref.2}.
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, probably
CC interacts with other sulfur acceptors. {ECO:0000255|HAMAP-
CC Rule:MF_00331, ECO:0000269|PubMed:10891064, ECO:0000269|PubMed:9582371,
CC ECO:0000269|Ref.2}.
CC -!- INTERACTION:
CC O31269; O31270: iscU; NbExp=3; IntAct=EBI-15710417, EBI-15710405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:9582371}.
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; AF010139; AAC24472.1; -; Genomic_DNA.
DR PIR; T44281; T44281.
DR AlphaFoldDB; O31269; -.
DR SMR; O31269; -.
DR DIP; DIP-46129N; -.
DR IntAct; O31269; 1.
DR UniPathway; UPA00266; -.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Pyridoxal phosphate; Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9582371"
FT CHAIN 2..404
FT /note="Cysteine desulfurase IscS"
FT /id="PRO_0000150260"
FT ACT_SITE 328
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305"
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, ECO:0000305"
SQ SEQUENCE 404 AA; 44600 MW; 242DCD4237493993 CRC64;
MKLPIYLDYS ATTPVDPRVA QKMCECLTME GNFGNPASRS HVFGWKAEEA VENARRQVAE
LVNADPREIV WTSGATESDN LAIKGVAHFN ASKGKHIITS KIEHKAVLDT TRQLEREGFE
VTYLEPGEDG LITPAMVAAA LREDTILVSV MHVNNEIGTV NDIAAIGELT RSRGVLYHVD
AAQSTGKVAI DLERMKVDLM SFSAHKTYGP KGIGALYVRR KPRVRLEAQM HGGGHERGMR
SGTLATHQIV GMGEAFRIAR EEMAAESRRI AGLSHRFHEQ VSTLEEVYLN GSATARVPHN
LNLSFNYVEG ESLIMSLRDL AVSSGSACTS ASLEPSYVLR ALGRNDELAH SSIRFTFGRF
TTEEEVDYAA RKVCEAVGKL RELSPLWDMY KDGVDLSKIE WQAH
