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Database: UniProt
Entry: Q93PT5_9CYAN
LinkDB: Q93PT5_9CYAN
Original site: Q93PT5_9CYAN 
ID   Q93PT5_9CYAN            Unreviewed;       108 AA.
AC   Q93PT5;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:AAK83134.1};
OS   unidentified marine bacterial clone HT1909.
OC   Bacteria; Cyanobacteriota; environmental samples.
OX   NCBI_TaxID=144381 {ECO:0000313|EMBL:AAK83134.1};
RN   [1] {ECO:0000313|EMBL:AAK83134.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11493920; DOI=10.1038/35088063;
RA   Zehr J.P., Waterbury J., Turner P.J., Montoya J., Omoregie E.,
RA   Steward G.F., Hansen A., Karl D.M.;
RT   "Unicellular cyanobacteria fix N2 in the subtropical North Pacific Ocean.";
RL   Nature 412:635-638(2001).
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}.
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DR   EMBL; AF299425; AAK83134.1; -; mRNA.
DR   AlphaFoldDB; Q93PT5; -.
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; PS51026; NIFH_FRXC_3; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAK83134.1"
FT   NON_TER         108
FT                   /evidence="ECO:0000313|EMBL:AAK83134.1"
SQ   SEQUENCE   108 AA;  11635 MW;  D0553128790D1F47 CRC64;
     STRLMLHCKA QTTVLHLAAE RGTVEDIELD EVVIPGYNNV LCVESGGPEP GVGCAGRGII
     TAINFLEEEG AYENLDFVSY DVLGDVVCVC FAMPIREGKA QEIYIVTS
//
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