(data stored in ACNUC7421 zone)

SWISSPROT: D4H6V6_DENA2

ID   D4H6V6_DENA2            Unreviewed;       290 AA.
AC   D4H6V6;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
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=Dacet_1046 {ECO:0000313|EMBL:ADD67822.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / N2460).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67822.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD67822.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / N2460 {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Detter J.C., Brettin T., Spring S.,
RA   Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
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:
CC       Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] =
CC         16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-
CC         [ferredoxin] + 16 phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, ChEBI:CHEBI:18276,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         EC=1.18.6.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00533,
CC         ECO:0000256|SAAS:SAAS01116923};
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-101 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}.
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DR   EMBL; CP001968; ADD67822.1; -; Genomic_DNA.
DR   RefSeq; WP_013010353.1; NC_013943.1.
DR   STRING; 522772.Dacet_1046; -.
DR   EnsemblBacteria; ADD67822; ADD67822; Dacet_1046.
DR   KEGG; dap:Dacet_1046; -.
DR   eggNOG; ENOG4105DSM; Bacteria.
DR   eggNOG; COG1348; LUCA.
DR   HOGENOM; HOG000228826; -.
DR   KO; K02588; -.
DR   OMA; PGDIVCG; -.
DR   OrthoDB; 729012at2; -.
DR   BioCyc; DACE522772:G1GHO-1051-MONOMER; -.
DR   Proteomes; UP000002012; 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;
DR   PRODOM; D4H6V6.
DR   SWISS-2DPAGE; D4H6V6.
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   Complete proteome {ECO:0000313|Proteomes:UP000002012};
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   ECO:0000313|EMBL:ADD67822.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00533}.
FT   METAL        98     98       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   METAL       133    133       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   MOD_RES     101    101       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00533,
FT                                ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   290 AA;  31614 MW;  28052A2D428DABF9 CRC64;
     MALRQIAFYG KGGIGKSTTS QNTLAAMAEM GKKIMIVGCD PKADSTRLIL HSKAQSTIME
     LAAEAGSVED LELDDVLKAG YLDIRCVEAG GPEPGVGCAG RGVITAINFL EEEGAYEEDL
     DFVSYDVLGD VVCGGFAMPI REGKAQEIYI VTSGEMMAMY AANNISKGIL KYANSGGVRL
     AGLICNERQT DREDELISEL ASKINTQMIH FVPRDNIVQH AELRRMTVVE YDGKCKQADE
     YRTLANKIIN NKMFNIPTPV SMQELEDLLM EFGIITEDDE AIVGKKAHEA
//

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