GenomeNet

Database: UniProt
Entry: K9R2G4_NOSS7
LinkDB: K9R2G4_NOSS7
Original site: K9R2G4_NOSS7 
ID   K9R2G4_NOSS7            Unreviewed;       324 AA.
AC   K9R2G4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   28-MAR-2018, entry version 36.
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=Nos7524_5546 {ECO:0000313|EMBL:AFY51257.1};
OS   Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY51257.1, ECO:0000313|Proteomes:UP000010378};
RN   [1] {ECO:0000313|Proteomes:UP000010378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E.,
RA   Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA   Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA   Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA   Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-
RT   driven genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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       ECO:0000256|SAAS:SAAS00692418}.
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       ECO:0000256|SAAS:SAAS00700909}.
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-104 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,
CC       ECO:0000256|SAAS:SAAS00700907}.
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; CP003552; AFY51257.1; -; Genomic_DNA.
DR   RefSeq; WP_015141658.1; NC_019684.1.
DR   EnsemblBacteria; AFY51257; AFY51257; Nos7524_5546.
DR   KEGG; nop:Nos7524_5546; -.
DR   PATRIC; fig|28072.8.peg.6091; -.
DR   KO; K02588; -.
DR   OMA; ILHCKAQ; -.
DR   OrthoDB; POG091H0230; -.
DR   Proteomes; UP000010378; 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, ECO:0000256|SAAS:SAAS00700918};
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, ECO:0000256|SAAS:SAAS00700908};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010378};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00533, ECO:0000256|RuleBase:RU003688,
KW   ECO:0000256|SAAS:SAAS00700910};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700920};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700915};
KW   Nitrogen fixation {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|SAAS:SAAS00692421};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700911};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00533,
KW   ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS00700919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT   NP_BIND      13     20       ATP. {ECO:0000256|HAMAP-Rule:MF_00533}.
FT   COILED      276    296       {ECO:0000256|SAM:Coils}.
FT   METAL       101    101       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   METAL       135    135       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   MOD_RES     104    104       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00533,
FT                                ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   324 AA;  35437 MW;  0A939759E49F0204 CRC64;
     MSDDRIRQIA FYGKGGIGKS TTSQNTLAAM AEMGKRILIV GCDPKADSTR LILHCKAQTT
     VLHLAAEKGA VEDLELEEVV IEGFRGIRCV ESGGPEPGVG CAGRGIITAI NFLEENGAYQ
     NLDFVSYDVL GDVVCGGFAM PIREGKAQEI YIVTSGEMMA MFAANNISRG ILKYAHSGGV
     RLGGLICNSR KTDREWDLIS ELAKRISTQM IHFVPRNNIV QHAELRRMTV NEYAPDSDQA
     HEYRALATKI INNDFMAVPT PLEMDELEDL LIEFGILESD EQVQKLTATA QAQEEQEKIQ
     EDAEGEALEA LAKGNVEIVS GDKK
//
DBGET integrated database retrieval system