ID Q1KX99_MASLA Unreviewed; 267 AA.
AC Q1KX99;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=nitrogenase {ECO:0000256|ARBA:ARBA00012773};
DE EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773};
DE AltName: Full=Nitrogenase component II {ECO:0000256|ARBA:ARBA00029951};
DE AltName: Full=Nitrogenase reductase {ECO:0000256|ARBA:ARBA00033027};
DE Flags: Fragment;
GN Name=nifH {ECO:0000313|EMBL:ABD49273.1};
OS Mastigocladus laminosus (Fischerella sp.).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocladus.
OX NCBI_TaxID=83541 {ECO:0000313|EMBL:ABD49273.1};
RN [1] {ECO:0000313|EMBL:ABD49273.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B12A {ECO:0000313|EMBL:ABD49273.1}, B13B
RC {ECO:0000313|EMBL:ABD49259.1}, B15A {ECO:0000313|EMBL:ABD49255.1}, B2B
RC {ECO:0000313|EMBL:ABD49257.1}, B2C {ECO:0000313|EMBL:ABD49267.1}, B2D
RC {ECO:0000313|EMBL:ABD49261.1}, B3A {ECO:0000313|EMBL:ABD49265.1}, B3D
RC {ECO:0000313|EMBL:ABD49271.1}, B4B {ECO:0000313|EMBL:ABD49269.1}, B6A
RC {ECO:0000313|EMBL:ABD49263.1}, W11D {ECO:0000313|EMBL:ABD49253.1},
RC W13D {ECO:0000313|EMBL:ABD49251.1}, W15C
RC {ECO:0000313|EMBL:ABD49243.1}, W16C {ECO:0000313|EMBL:ABD49239.1},
RC W17B {ECO:0000313|EMBL:ABD49249.1}, W17C
RC {ECO:0000313|EMBL:ABD49235.1}, W1C {ECO:0000313|EMBL:ABD49247.1}, W23B
RC {ECO:0000313|EMBL:ABD49245.1}, W25B {ECO:0000313|EMBL:ABD49241.1}, and
RC W7C {ECO:0000313|EMBL:ABD49237.1};
RX PubMed=16597984; DOI=10.1128/AEM.72.4.2793-2800.2006;
RA Miller S.R., Purugganan M.D., Curtis S.E.;
RT "Molecular population genetics and phenotypic diversification of two
RT populations of the thermophilic cyanobacterium Mastigocladus laminosus.";
RL Appl. Environ. Microbiol. 72:2793-2800(2006).
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 -!- PTM: The reversible ADP-ribosylation of Arg inactivates the nitrogenase
CC reductase and regulates nitrogenase activity.
CC {ECO:0000256|PIRSR:PIRSR605977-50}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|RuleBase:RU003688}.
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DR EMBL; DQ385910; ABD49235.1; -; Genomic_DNA.
DR EMBL; DQ385911; ABD49237.1; -; Genomic_DNA.
DR EMBL; DQ385912; ABD49239.1; -; Genomic_DNA.
DR EMBL; DQ385913; ABD49241.1; -; Genomic_DNA.
DR EMBL; DQ385914; ABD49243.1; -; Genomic_DNA.
DR EMBL; DQ385915; ABD49245.1; -; Genomic_DNA.
DR EMBL; DQ385916; ABD49247.1; -; Genomic_DNA.
DR EMBL; DQ385917; ABD49249.1; -; Genomic_DNA.
DR EMBL; DQ385918; ABD49251.1; -; Genomic_DNA.
DR EMBL; DQ385919; ABD49253.1; -; Genomic_DNA.
DR EMBL; DQ385920; ABD49255.1; -; Genomic_DNA.
DR EMBL; DQ385921; ABD49257.1; -; Genomic_DNA.
DR EMBL; DQ385922; ABD49259.1; -; Genomic_DNA.
DR EMBL; DQ385923; ABD49261.1; -; Genomic_DNA.
DR EMBL; DQ385924; ABD49263.1; -; Genomic_DNA.
DR EMBL; DQ385925; ABD49265.1; -; Genomic_DNA.
DR EMBL; DQ385926; ABD49267.1; -; Genomic_DNA.
DR EMBL; DQ385927; ABD49269.1; -; Genomic_DNA.
DR EMBL; DQ385928; ABD49271.1; -; Genomic_DNA.
DR EMBL; DQ385929; ABD49273.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KX99; -.
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 GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd02040; NifH; 1.
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; IPR005977; Nitrogenase_Fe_NifH.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01287; nifH; 1.
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 PIRSF; PIRSF000363; Nitrogenase_iron; 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 ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765,
KW ECO:0000256|PIRSR:PIRSR605977-50};
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 Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003688};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003688}.
FT MOD_RES 75
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000256|PIRSR:PIRSR605977-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABD49273.1"
SQ SEQUENCE 267 AA; 29192 MW; CA149B8FE7A65236 CRC64;
MAEMGQRILI VGCDPKADST RLMLHSKAQT TVLHLAAERG AVEDLELEEV MLTGFRGVKC
VESGGPEPGV GCAGRGIITA INFLEENGAY QDLDFVSYDV LGDVVCGGFA MPIREGKAQE
IYIVTSGEMM AMYAANNIAR GILKYAHSGG VRLGGLICNS RKVDREIELI ETLAEKLNTQ
MIHFVPRDNI VQHAELRRMT VNEYAPDSNQ ANEYRALAKK IINNTKLTIP TPLEMDELEA
LLIEYGILDD DTKHADIIGK PAEATAK
//
