ID Q5MQ55_9CYAN Unreviewed; 108 AA.
AC Q5MQ55;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 56.
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:AAV51288.1};
OS uncultured cyanobacterium.
OC Bacteria; Cyanobacteriota; environmental samples.
OX NCBI_TaxID=1211 {ECO:0000313|EMBL:AAV51288.1};
RN [1] {ECO:0000313|EMBL:AAV51288.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15574936; DOI=10.1128/AEM.70.12.7355-7364.2004;
RA Mazard S.L., Fuller N.J., Orcutt K.M., Bridle O., Scanlan D.J.;
RT "PCR analysis of the distribution of unicellular cyanobacterial diazotrophs
RT in the Arabian Sea.";
RL Appl. Environ. Microbiol. 70:7355-7364(2004).
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}.
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; AY621713; AAV51288.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5MQ55; -.
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:AAV51288.1"
FT NON_TER 108
FT /evidence="ECO:0000313|EMBL:AAV51288.1"
SQ SEQUENCE 108 AA; 11304 MW; DF58205934285015 CRC64;
STRLILNAKA QTTVLHVAAE RGAVEDVELD EVLKPGFGGI KCVESGGPEP GVGCAGRGII
TAINFLEEEG AYTDLDFVSY DVLGDVVCGG FAMPIRGNKA QEIYIVCS
//