ID NIFS_AZOVI Reviewed; 402 AA.
AC P05341;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Cysteine desulfurase NifS {ECO:0000303|PubMed:8464885};
DE EC=2.8.1.7 {ECO:0000269|PubMed:8464885};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000303|PubMed:8464885};
GN Name=nifS {ECO:0000303|PubMed:3040672};
OS Azotobacter vinelandii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3040672; DOI=10.1128/jb.169.9.4024-4029.1987;
RA Beynon J., Ally A., Cannon M., Cannon F., Jacobson M.R., Cash V.L.,
RA Dean D.R.;
RT "Comparative organization of nitrogen fixation-specific genes from
RT Azotobacter vinelandii and Klebsiella pneumoniae: DNA sequence of the
RT nifUSV genes.";
RL J. Bacteriol. 169:4024-4029(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT "Physical and genetic map of the major nif gene cluster from Azotobacter
RT vinelandii.";
RL J. Bacteriol. 171:1017-1027(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-6, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=8464885; DOI=10.1073/pnas.90.7.2754;
RA Zheng L., White R.H., Cash V.L., Jack R.F., Dean D.R.;
RT "Cysteine desulfurase activity indicates a role for NIFS in metallocluster
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2754-2758(1993).
RN [4]
RP PROTEIN SEQUENCE OF 315-326, MUTAGENESIS OF CYS-325, AND ACTIVE SITE.
RX PubMed=8161529; DOI=10.1021/bi00181a031;
RA Zheng L., White R.H., Cash V.L., Dean D.R.;
RT "Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene
RT product.";
RL Biochemistry 33:4714-4720(1994).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC to produce alanine. Seems to participate in the biosynthesis of the
CC nitrogenase metalloclusters by providing the inorganic sulfur required
CC for the Fe-S core formation. {ECO:0000269|PubMed:8464885}.
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:0000269|PubMed:8464885};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:8464885};
CC -!- ACTIVITY REGULATION: Inhibited by equimolar concentrations of p-
CC chloromercuribenzoic acid, iodoacetamide or N-ethylmaleimide.
CC {ECO:0000269|PubMed:8464885}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8464885}.
CC -!- DISRUPTION PHENOTYPE: Fixes nitrogen very poorly; has very slow
CC diazotrophic growth on nitrogen-free agar plates. A double nifS-nifV
CC deletion no longer fixes nitrogen. {ECO:0000269|PubMed:2644218}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M17349; AAA22168.1; -; Genomic_DNA.
DR EMBL; M20568; AAA64726.1; -; Genomic_DNA.
DR PIR; S29757; S29757.
DR AlphaFoldDB; P05341; -.
DR SMR; P05341; -.
DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:CACAO.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 1.
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 InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR017772; Cys_deSase_NifS_bac/arc.
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 NCBIfam; TIGR03402; FeS_nifS; 1.
DR PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Pyridoxal phosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8464885"
FT CHAIN 2..402
FT /note="Cysteine desulfurase NifS"
FT /id="PRO_0000150252"
FT ACT_SITE 325
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:8161529"
FT BINDING 72..73
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 151
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 199..201
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 325
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:0000250|UniProtKB:O29689"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT MUTAGEN 325
FT /note="C->A: Loss of cysteine desulfurization; loss of
FT reactivity toward alkylation."
FT /evidence="ECO:0000269|PubMed:8161529"
FT CONFLICT 39
FT /note="F -> L (in Ref. 1; AAA22168)"
FT /evidence="ECO:0000305"
SQ 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
//
