位置:首页 > 蛋白库 > NIFH2_AZOVI
NIFH2_AZOVI
ID   NIFH2_AZOVI             Reviewed;         290 AA.
AC   P15335;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Nitrogenase iron protein 2;
DE            EC=1.18.6.1;
DE   AltName: Full=Nitrogenase Fe protein 2;
DE   AltName: Full=Nitrogenase component II;
DE   AltName: Full=Nitrogenase reductase;
GN   Name=vnfH; Synonyms=nifH2;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3226421; DOI=10.1007/bf00340189;
RA   Raina R., Reddy A., Ghosal D., Das H.K.;
RT   "Characterization of the gene for the Fe-protein of the vanadium dependent
RT   alternative nitrogenase of Azotobacter vinelandii and construction of a Tn5
RT   mutant.";
RL   Mol. Gen. Genet. 214:121-127(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA;
RX   PubMed=2345152; DOI=10.1128/jb.172.6.3400-3408.1990;
RA   Joerger R.D., Loveless T.M., Pau R.N., Mitchenall L.A., Simon B.H.,
RA   Bishop P.E.;
RT   "Nucleotide sequences and mutational analysis of the structural genes for
RT   nitrogenase 2 of Azotobacter vinelandii.";
RL   J. Bacteriol. 172:3400-3408(1990).
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the iron
CC       protein (component 2) and a component 1 which is either a molybdenum-
CC       iron protein, a vanadium-iron, or an iron-iron protein.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC         ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC         phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=1.18.6.1;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per dimer.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- PTM: The reversible ADP-ribosylation of Arg-101 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: This subunit is associated with the vanadium-iron
CC       nitrogenase component 2.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {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; X13519; CAA31867.1; -; Genomic_DNA.
DR   EMBL; M32371; AAA22170.1; -; Genomic_DNA.
DR   PIR; A35405; A35405.
DR   AlphaFoldDB; P15335; -.
DR   SMR; P15335; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00533; NifH; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR005977; Nitrogenase_Fe_NifH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01287; nifH; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ADP-ribosylation; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..290
FT                   /note="Nitrogenase iron protein 2"
FT                   /id="PRO_0000139491"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         98
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         101
FT                   /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT                   ribosyltransferase"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        67
FT                   /note="W -> S (in Ref. 2; AAA22170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="G -> A (in Ref. 2; AAA22170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="S -> I (in Ref. 2; AAA22170)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   290 AA;  31102 MW;  1819DB93BFFC2A05 CRC64;
     MALRQCAIYG KGGIGKSTTT QNLVAALAEA GKKVMIVGCD PKADSTRLIL HSKAQGTVME
     MAASAGWVED LELEDVLQIG FGGVKCVESG GPEPGVGCAG RGVITAINFL EEEGAYSDDL
     DFVFYDVLGD VVCGGFAMPI RENKAQEIYI VCSGEMMAMY AANNIAKGSV KYAHSGSVRL
     GGLICNSRKT DREDELIMAL AAKIGTQMIH FVPRDNVVQH AEIRRMTVIE YDPKAGQADE
     YRALARKIVD NKLLVIPNPA SMEELEELLM EFGIMEVEDE SVVGKAAAEG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024