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NIFS_AZOVI
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   03-AUG-2022, entry version 104.
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; Proteobacteria; 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}.
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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:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03402; FeS_nifS; 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
 
 
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