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Database: UniProt
Entry: D7DT99_METV3
LinkDB: D7DT99_METV3
Original site: D7DT99_METV3 
ID   D7DT99_METV3            Unreviewed;       278 AA.
AC   D7DT99;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   28-MAR-2018, entry version 45.
DE   RecName: Full=Nitrogenase iron protein {ECO:0000256|HAMAP-Rule:MF_00533};
DE            EC=1.18.6.1 {ECO:0000256|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase Fe protein {ECO:0000256|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase component II {ECO:0000256|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase reductase {ECO:0000256|HAMAP-Rule:MF_00533};
GN   Name=nifH {ECO:0000256|HAMAP-Rule:MF_00533};
GN   OrderedLocusNames=Mvol_0700 {ECO:0000313|EMBL:ADI36359.1};
OS   Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36359.1, ECO:0000313|Proteomes:UP000007722};
RN   [1] {ECO:0000313|EMBL:ADI36359.1, ECO:0000313|Proteomes:UP000007722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanococcus voltae A3.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the
CC       iron protein and the molybdenum-iron protein. {ECO:0000256|HAMAP-
CC       Rule:MF_00533}.
CC   -!- CATALYTIC ACTIVITY: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP
CC       + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00533}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00533};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC       Rule:MF_00533};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00533}.
CC   -!- PTM: The reversible ADP-ribosylation of Arg inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000256|PIRSR:PIRSR605977-50}.
CC   -!- PTM: The reversible ADP-ribosylation of Arg-97 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00533}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|HAMAP-Rule:MF_00533, ECO:0000256|RuleBase:RU003688}.
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DR   EMBL; CP002057; ADI36359.1; -; Genomic_DNA.
DR   RefSeq; WP_013180087.1; NC_014222.1.
DR   ProteinModelPortal; D7DT99; -.
DR   STRING; 456320.Mvol_0700; -.
DR   EnsemblBacteria; ADI36359; ADI36359; Mvol_0700.
DR   GeneID; 9275922; -.
DR   KEGG; mvo:Mvol_0700; -.
DR   eggNOG; arCOG00590; Archaea.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228825; -.
DR   KO; K02588; -.
DR   OMA; EVDFHHE; -.
DR   OrthoDB; POG093Z00RZ; -.
DR   BioCyc; MVOL456320:G1FZ2-698-MONOMER; -.
DR   Proteomes; UP000007722; Chromosome.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
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   CDD; cd02040; NifH; 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 {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688};
KW   ADP-ribosylation {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|PIRSR:PIRSR605977-50};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007722};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00533, ECO:0000256|RuleBase:RU003688};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688};
KW   Nitrogen fixation {ECO:0000256|HAMAP-Rule:MF_00533};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000313|EMBL:ADI36359.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007722}.
FT   NP_BIND       8     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00533}.
FT   METAL        94     94       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   METAL       130    130       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   MOD_RES      97     97       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00533,
FT                                ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   278 AA;  30412 MW;  627C2B88EDAE6762 CRC64;
     MRKFCIYGKG GIGKSTNVGN MAAALAEDGK KVLVVGCDPK ADSTRTLMHG KINTVLDTFR
     DKGPEYMKIE DIVYEGFNGV YCVESGGPEP GVGCAGRGVI TAVDMLDRLG VYDELKPDVV
     MYDILGDVVC GGFAMPLQKR LAEDVYIVTT CDPMAIYAAN NICKGIQRYG NRGKIALGGI
     IYNGRSVVDE PEIIDKFVQG INTQVMGKIP MSNIITKAEL RKQTTIEYAP DSEIANKFRE
     LANAIYENKK TTIPTPLSEQ GLDDLTESIE ELVRKKYE
//
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