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Cysteine desulfurase IscS (EC 2.8.1.7)

 ISCS_AZOVI              Reviewed;         404 AA.
O31269;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 95.
RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000303|PubMed:9582371};
EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:9582371};
Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331};
Azotobacter vinelandii.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Azotobacter.
NCBI_TaxID=354;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-23; 3-18;
241-257; 319-340 AND 382-391, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
ACTIVITY REGULATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
PubMed=9582371; DOI=10.1074/jbc.273.21.13264;
Zheng L., Cash V.L., Flint D.H., Dean D.R.;
"Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-
fdx gene cluster from Azotobacter vinelandii.";
J. Biol. Chem. 273:13264-13272(1998).
[2]
FUNCTION, INTERACTION WITH ISCU, SUBUNIT, PATHWAY, AND REACTION
MECHANISM.
STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
DOI=10.1021/ja9944195;
Agar J.N., Zheng L., Cash V.L., Dean D.R., Johnson M.K.;
"Role of the iscU protein in iron-sulfur cluster biosynthesis: IscS-
mediated assembly of a [Fe2S2] cluster in IscU.";
J. Am. Chem. Soc. 122:2136-2137(2000).
[3]
FUNCTION IN FE-S CLUSTER FORMATION, REACTION MECHANISM, AND SUBUNIT.
STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
PubMed=10891064; DOI=10.1021/bi000931n;
Agar J.N., Krebs C., Frazzon J., Huynh B.H., Dean D.R., Johnson M.K.;
"IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential
assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU.";
Biochemistry 39:7856-7862(2000).
-!- FUNCTION: Master enzyme that delivers sulfur to a number of
partners involved in Fe-S cluster assembly, tRNA modification or
cofactor biosynthesis. Catalyzes the removal of elemental sulfur
from cysteine to produce alanine via an enzyme-bound persulfide
intermediate. Functions as a sulfur delivery protein for Fe-S
cluster synthesis. Cluster assembly on IscU homodimers proceeds
sequentially from 1 2Fe-2S per dimer, to 2 2Fe-2S per dimer and
finally 1 4Fe-4S per dimer. {ECO:0000269|PubMed:10891064,
ECO:0000269|PubMed:9582371, ECO:0000269|Ref.2}.
-!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
sulfanyl-acceptor. {ECO:0000255|HAMAP-Rule:MF_00331,
ECO:0000269|PubMed:9582371}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000255|HAMAP-Rule:MF_00331,
ECO:0000269|PubMed:9582371};
-!- ACTIVITY REGULATION: Inhibited by equimolar N-iodoacetyl-N'-(5-
sulfo-1-naphthyl)ethylenediamine. {ECO:0000269|PubMed:9582371}.
-!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|Ref.2}.
-!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, probably
interacts with other sulfur acceptors. {ECO:0000255|HAMAP-
Rule:MF_00331, ECO:0000269|PubMed:10891064,
ECO:0000269|PubMed:9582371, ECO:0000269|Ref.2}.
-!- INTERACTION:
O31270:iscU; NbExp=3; IntAct=EBI-15710417, EBI-15710405;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
-!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
{ECO:0000269|PubMed:9582371}.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP-
Rule:MF_00331}.
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EMBL; AF010139; AAC24472.1; -; Genomic_DNA.
PIR; T44281; T44281.
ProteinModelPortal; O31269; -.
SMR; O31269; -.
DIP; DIP-46129N; -.
IntAct; O31269; 1.
PRIDE; O31269; -.
eggNOG; ENOG4105C3J; Bacteria.
eggNOG; COG1104; LUCA.
UniPathway; UPA00266; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-UniRule.
GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_00331; Cys_desulf_IscS; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
InterPro; IPR010240; Cys_deSase_IscS.
InterPro; IPR016454; Cysteine_dSase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF005572; NifS; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR02006; IscS; 1.
PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
1: Evidence at protein level;
2Fe-2S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
Metal-binding; Pyridoxal phosphate; Transferase; tRNA processing.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9582371}.
CHAIN 2 404 Cysteine desulfurase IscS.
/FTId=PRO_0000150260.
REGION 75 76 Pyridoxal phosphate binding.
{ECO:0000255|HAMAP-Rule:MF_00331}.
REGION 203 205 Pyridoxal phosphate binding.
{ECO:0000255|HAMAP-Rule:MF_00331}.
ACT_SITE 328 328 Cysteine persulfide intermediate.
{ECO:0000255|HAMAP-Rule:MF_00331,
ECO:0000305}.
METAL 328 328 Iron-sulfur (2Fe-2S); via persulfide
group; shared with IscU.
{ECO:0000255|HAMAP-Rule:MF_00331}.
BINDING 155 155 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00331}.
BINDING 183 183 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00331}.
BINDING 243 243 Pyridoxal phosphate. {ECO:0000255|HAMAP-
Rule:MF_00331}.
MOD_RES 206 206 N6-(pyridoxal phosphate)lysine.
{ECO:0000255|HAMAP-Rule:MF_00331,
ECO:0000305}.
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


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