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Database: UniProt
Entry: G4XRC1_9CYAN
LinkDB: G4XRC1_9CYAN
Original site: G4XRC1_9CYAN 
ID   G4XRC1_9CYAN            Unreviewed;        82 AA.
AC   G4XRC1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=nitrogenase {ECO:0000256|ARBA:ARBA00012773};
DE            EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773};
DE   Flags: Fragment;
GN   Name=nifH {ECO:0000313|EMBL:AEP26267.1};
OS   uncultured cyanobacterium.
OC   Bacteria; Cyanobacteriota; environmental samples.
OX   NCBI_TaxID=1211 {ECO:0000313|EMBL:AEP26267.1};
RN   [1] {ECO:0000313|EMBL:AEP26267.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DGGE gel band DAR-D33 {ECO:0000313|EMBL:AEP26267.1}, and DGGE
RC   gel band DAR-R66 {ECO:0000313|EMBL:AEP26255.1};
RX   PubMed=23754717; DOI=10.1111/1758-2229.12031;
RA   Hamisi M., Diez B., Lyimo T., Ininbergs K., Bergman B.;
RT   "Epiphytic cyanobacteria of the seagrass Cymodocea rotundata: diversity,
RT   diel nifH expression and nitrogenase activity.";
RL   Environ. Microbiol. Rep. 5:367-376(2013).
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the iron
CC       protein and the molybdenum-iron protein.
CC       {ECO:0000256|ARBA:ARBA00002234}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC         ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC         phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=1.18.6.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000805};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC       {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|RuleBase:RU003688}.
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DR   EMBL; JF896656; AEP26255.1; -; Genomic_DNA.
DR   EMBL; JF896668; AEP26267.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4XRC1; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-EC.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR   PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PRINTS; PR00091; NITROGNASEII.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003688};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003688};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003688};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003688};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003688};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003688};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003688}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEP26267.1"
FT   NON_TER         82
FT                   /evidence="ECO:0000313|EMBL:AEP26267.1"
SQ   SEQUENCE   82 AA;  8771 MW;  D56A939CC0D89EC3 CRC64;
     EDVELDEVLK DGFAGIRCVE SGGPEPGVGC AGRGIITAIN FLEEEGAYKD LDFVSYDVLG
     DVVCGGFAMP IRENKAQEIY IV
//
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