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Database: UniProt
Entry: A0A0F2JJ95_9FIRM
LinkDB: A0A0F2JJ95_9FIRM
Original site: A0A0F2JJ95_9FIRM 
ID   A0A0F2JJ95_9FIRM        Unreviewed;       275 AA.
AC   A0A0F2JJ95;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   10-OCT-2018, entry version 20.
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   ORFNames=UF75_0216 {ECO:0000313|EMBL:KJR49376.1};
OS   Desulfosporosinus sp. I2.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR49376.1, ECO:0000313|Proteomes:UP000033442};
RN   [1] {ECO:0000313|EMBL:KJR49376.1, ECO:0000313|Proteomes:UP000033442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I2 {ECO:0000313|EMBL:KJR49376.1,
RC   ECO:0000313|Proteomes:UP000033442};
RA   Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V.,
RA   Ravin N.V.;
RL   Submitted (FEB-2015) 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       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-99 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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJR49376.1}.
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DR   EMBL; JYNH01000002; KJR49376.1; -; Genomic_DNA.
DR   RefSeq; WP_045572734.1; NZ_JYNH01000002.1.
DR   EnsemblBacteria; KJR49376; KJR49376; UF75_0216.
DR   PATRIC; fig|1617025.3.peg.221; -.
DR   Proteomes; UP000033442; Unassembled WGS sequence.
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:UP000033442};
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:UP000033442}.
FT   NP_BIND       8     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00533}.
FT   COILED      229    249       {ECO:0000256|SAM:Coils}.
FT   METAL        96     96       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   METAL       131    131       Iron-sulfur (4Fe-4S); shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00533}.
FT   MOD_RES      99     99       ADP-ribosylarginine; by dinitrogenase
FT                                reductase ADP-ribosyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_00533,
FT                                ECO:0000256|PIRSR:PIRSR605977-50}.
SQ   SEQUENCE   275 AA;  30160 MW;  9A70B210EAAB9F57 CRC64;
     MRQIAIYGKG GIGKSTTTQN TVVALAEMGR KVTIVGCDPK ADSTRLILHS KAQTTVMDLA
     RERGTVEDLE LDEVLVEGYL GVRCAESGGP EPGVGCAGRG VITAINFLEE NGAYTADTDY
     VFYDVLGDVV CGGFAMPIRE NKAKEIYIVT SGEMMAMYAA NNISKGILKY AQTGTVRLGG
     LICNSRQTDK ENELIEALAK SLNTQMIHFM PRDNEVQRAE VRKMTVIEYN STHKQADEYR
     ALAQKIENNT MMTIPTPLSM DALEDLMMEF GIMDM
//
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