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Database: UniProt
Entry: A0A0K8JH24_9FIRM
LinkDB: A0A0K8JH24_9FIRM
Original site: A0A0K8JH24_9FIRM 
ID   A0A0K8JH24_9FIRM        Unreviewed;       272 AA.
AC   A0A0K8JH24;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-MAR-2018, entry version 15.
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=nifH1 {ECO:0000313|EMBL:CUH96902.1};
GN   Synonyms=nifH {ECO:0000256|HAMAP-Rule:MF_00533};
GN   ORFNames=P22_3014 {ECO:0000313|EMBL:CUH96902.1};
OS   Propionispora sp. 2/2-37.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Propionispora.
OX   NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH96902.1, ECO:0000313|Proteomes:UP000041641};
RN   [1] {ECO:0000313|EMBL:CUH96902.1, ECO:0000313|Proteomes:UP000041641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2/2 {ECO:0000313|EMBL:CUH96902.1};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-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-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,
CC       ECO:0000256|SAAS:SAAS00700907}.
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DR   EMBL; CYSP01000014; CUH96902.1; -; Genomic_DNA.
DR   RefSeq; WP_054261037.1; NZ_CYSP01000014.1.
DR   EnsemblBacteria; CUH96902; CUH96902; P22_3014.
DR   Proteomes; UP000041641; 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   Complete proteome {ECO:0000313|Proteomes:UP000041641};
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:CUH96902.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041641}.
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       129    129       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   272 AA;  29455 MW;  580823411ECD08FE CRC64;
     MRQVAIYGKG GIGKSTTTQN TVAALAEAGK KVMVVGCDPK ADSTRLLLNG LCQKTVLDTL
     RDEGDDIELE DILKPGFKGT MCVESGGPEP GVGCAGRGII TSINLLESLG AYTSDLDYVF
     YDVLGDVVCG GFAMPIREGK AQEIYIVASG ELMALYAANN ISKGIQKYAA TGGVRLGGII
     CNSRKVDREL DLLENFATEL GSQLIHFVPR DNVVQRAEIN KKTVIDYDPK EDQADEYRKL
     AMAINQNKMF VVPKPMTQDR LEELMMSYGI LG
//
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