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Cysteine desulfurase NifS (EC 2.8.1.7) (Nitrogenase metalloclusters biosynthesis protein NifS)

 NIFS_AZOVI              Reviewed;         402 AA.
P05341;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
05-JUL-2017, entry version 93.
RecName: Full=Cysteine desulfurase NifS {ECO:0000303|PubMed:8464885};
EC=2.8.1.7 {ECO:0000269|PubMed:8464885};
AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000303|PubMed:8464885};
Name=nifS {ECO:0000303|PubMed:3040672};
Azotobacter vinelandii.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Azotobacter.
NCBI_TaxID=354;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3040672; DOI=10.1128/jb.169.9.4024-4029.1987;
Beynon J., Ally A., Cannon M., Cannon F., Jacobson M.R., Cash V.L.,
Dean D.R.;
"Comparative organization of nitrogen fixation-specific genes from
Azotobacter vinelandii and Klebsiella pneumoniae: DNA sequence of the
nifUSV genes.";
J. Bacteriol. 169:4024-4029(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
PubMed=2644218;
Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A.,
Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.;
"Physical and genetic map of the major nif gene cluster from
Azotobacter vinelandii.";
J. Bacteriol. 171:1017-1027(1989).
[3]
PROTEIN SEQUENCE OF 2-6, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
ENZYME REGULATION, AND SUBUNIT.
PubMed=8464885; DOI=10.1073/pnas.90.7.2754;
Zheng L., White R.H., Cash V.L., Jack R.F., Dean D.R.;
"Cysteine desulfurase activity indicates a role for NIFS in
metallocluster biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 90:2754-2758(1993).
[4]
PROTEIN SEQUENCE OF 315-326, MUTAGENESIS OF CYS-325, AND ACTIVE SITE.
PubMed=8161529; DOI=10.1021/bi00181a031;
Zheng L., White R.H., Cash V.L., Dean D.R.;
"Mechanism for the desulfurization of L-cysteine catalyzed by the nifS
gene product.";
Biochemistry 33:4714-4720(1994).
-!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from
cysteine to produce alanine. Seems to participate in the
biosynthesis of the nitrogenase metalloclusters by providing the
inorganic sulfur required for the Fe-S core formation.
{ECO:0000269|PubMed:8464885}.
-!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
sulfanyl-acceptor. {ECO:0000269|PubMed:8464885}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:8464885};
-!- ENZYME REGULATION: Inhibited by equimolar concentrations of p-
chloromercuribenzoic acid, iodoacetamide or N-ethylmaleimide.
{ECO:0000269|PubMed:8464885}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8464885}.
-!- DISRUPTION PHENOTYPE: Fixes nitrogen very poorly; has very slow
diazotrophic growth on nitrogen-free agar plates. A double nifS-
nifV deletion no longer fixes nitrogen.
{ECO:0000269|PubMed:2644218}.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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EMBL; M17349; AAA22168.1; -; Genomic_DNA.
EMBL; M20568; AAA64726.1; -; Genomic_DNA.
PIR; S29757; S29757.
ProteinModelPortal; P05341; -.
SMR; P05341; -.
eggNOG; ENOG4105C3J; Bacteria.
eggNOG; COG1104; LUCA.
GO; GO:0031071; F:cysteine desulfurase activity; IDA:CACAO.
GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
InterPro; IPR017772; Cys_deSase_NifS_bac/arc.
InterPro; IPR016454; Cysteine_dSase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF005572; NifS; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR03402; FeS_nifS; 1.
PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
1: Evidence at protein level;
Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
Nitrogen fixation; Pyridoxal phosphate; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8464885}.
CHAIN 2 402 Cysteine desulfurase NifS.
/FTId=PRO_0000150252.
REGION 72 73 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P0A6B9}.
REGION 199 201 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P0A6B9}.
ACT_SITE 325 325 Cysteine persulfide intermediate.
{ECO:0000269|PubMed:8161529}.
METAL 325 325 Iron-sulfur (2Fe-2S); via persulfide
group; shared with IscU.
{ECO:0000250|UniProtKB:O29689}.
BINDING 151 151 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:O29689}.
BINDING 179 179 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P0A6B9}.
BINDING 237 237 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P0A6B9}.
MOD_RES 202 202 N6-(pyridoxal phosphate)lysine.
{ECO:0000305}.
MUTAGEN 325 325 C->A: Loss of cysteine desulfurization;
loss of reactivity toward alkylation.
{ECO:0000269|PubMed:8161529}.
CONFLICT 39 39 F -> L (in Ref. 1; AAA22168).
{ECO:0000305}.
SEQUENCE 402 AA; 43599 MW; B994743764265DDC CRC64;
MADVYLDNNA TTRVDDEIVQ AMLPFFTEQF GNPSSLHSFG NQVGMALKKA RQSVQKLLGA
EHDSEILFTS CGTESDSTAI LSALKAQPER KTVITTVVEH PAVLSLCDYL ASEGYTVHKL
PVDKKGRLDL EHYASLLTDD VAVVSVMWAN NETGTLFPIE EMARLADDAG IMFHTDAVQA
VGKVPIDLKN SSIHMLSLCG HKLHAPKGVG VLYLRRGTRF RPLLRGGHQE RGRRAGTENA
ASIIGLGVAA ERALQFMEHE NTEVNALRDK LEAGILAVVP HAFVTGDPDN RLPNTANIAF
EYIEGEAILL LLNKVGIAAS SGSACTSGSL EPSHVMRAMD IPYTAAHGTV RFSLSRYTTE
EEIDRVIREV PPIVAQLRNV SPYWSGNGPV EDPGKAFAPV YG


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