NIFH2_TRIV2
ID NIFH2_TRIV2 Reviewed; 296 AA.
AC Q44484; Q3M590; Q44469;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nitrogenase iron protein 2;
DE EC=1.18.6.1;
DE AltName: Full=Nitrogenase Fe protein 2;
DE AltName: Full=Nitrogenase component II;
DE AltName: Full=Nitrogenase reductase;
GN Name=nifH2; OrderedLocusNames=Ava_4247;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7568132; DOI=10.1073/pnas.92.20.9358;
RA Thiel T., Lyons E.M., Erker J.C., Ernst A.;
RT "A second nitrogenase in vegetative cells of a heterocyst-forming
RT cyanobacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9358-9362(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=8709854; DOI=10.1111/j.1365-2958.1995.mmi_18020357.x;
RA Schrautemeier B., Neveling U., Schmitz S.;
RT "Distinct and differently regulated Mo-dependent nitrogen-fixing systems
RT evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC
RT 29413: characterization of the fdxH1/2 gene regions as part of the nif1/2
RT gene clusters.";
RL Mol. Microbiol. 18:357-369(1995).
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 -!- 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per dimer.;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- PTM: The reversible ADP-ribosylation of Arg-103 inactivates the
CC nitrogenase reductase and regulates nitrogenase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR EMBL; U49859; AAA93020.1; -; Genomic_DNA.
DR EMBL; U25160; AAC43540.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA23846.1; -; Genomic_DNA.
DR PIR; S70251; S70251.
DR AlphaFoldDB; Q44484; -.
DR SMR; Q44484; -.
DR STRING; 240292.Ava_4247; -.
DR EnsemblBacteria; ABA23846; ABA23846; Ava_4247.
DR KEGG; ava:Ava_4247; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_0_0_3; -.
DR OMA; YQGVKCV; -.
DR Proteomes; UP000002533; Chromosome.
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 Gene3D; 3.40.50.300; -; 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; ADP-ribosylation; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..296
FT /note="Nitrogenase iron protein 2"
FT /id="PRO_0000139484"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 171
FT /note="L -> W (in Ref. 1; AAA93020)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> V (in Ref. 1; AAA93020)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="Q -> P (in Ref. 1; AAA93020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 32208 MW; 761CB9AB74697B1F CRC64;
MIDNIRQIAF YGKGGIGKST TSQNTIAGLA EMGERIMIVG CDPKADSTRL MLHSKAQTTI
LHLAAERGAV EDLELDEVLL TGYQGVKCVE SGGPEPGVGC AGRGIITAIN FLEENGAYED
LDFVSYDVLG DVVCGGFAMP IREGKAQEIY IVCSGEMMAM YAANNIARGI LKYAHSGGVR
LGGLICNSRN VDREVELIEA LAERLNTQMI HFVPRNNVVQ HAELRRMTVI EYATEHPQAN
EYRTLAKKIK ENTKLTIPTP ISMDELEELL VEFGILGGEE EYQKAIAQDA GKAVVV
