NIFH1_RHOCA
ID NIFH1_RHOCA Reviewed; 295 AA.
AC P0CY95; P08718;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Nitrogenase iron protein 1;
DE EC=1.18.6.1;
DE AltName: Full=Nitrogenase Fe protein 1;
DE AltName: Full=Nitrogenase component II;
DE AltName: Full=Nitrogenase reductase;
GN Name=nifH;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3557130; DOI=10.1016/0378-1119(86)90354-9;
RA Schumann J.P., Waitches G.M., Scolnik P.A.;
RT "A DNA fragment hybridizing to a nif probe in Rhodobacter capsulatus is
RT homologous to a 16S rRNA gene.";
RL Gene 48:81-92(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=7693551; DOI=10.1016/0378-1119(93)90222-o;
RA Willison J.C., Pierrard J., Huebner P.;
RT "Sequence and transcript analysis of the nitrogenase structural gene operon
RT (nifHDK) of Rhodobacter capsulatus: evidence for intramolecular processing
RT of nifHDK mRNA.";
RL Gene 133:39-46(1993).
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. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- PTM: The reversible ADP-ribosylation of Arg-102 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; M15270; AAA26140.1; -; Genomic_DNA.
DR EMBL; X63352; CAA44954.1; -; Genomic_DNA.
DR PIR; JN0888; JN0888.
DR RefSeq; WP_013066316.1; NZ_VIBE01000010.1.
DR AlphaFoldDB; P0CY95; -.
DR SMR; P0CY95; -.
DR GeneID; 31489522; -.
DR OMA; YVCDYYL; -.
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..295
FT /note="Nitrogenase iron protein 1"
FT /id="PRO_0000139527"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 99
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 133
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 102
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 66
FT /note="A -> V (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="V -> L (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="K -> R (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="A -> S (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="M -> C (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> V (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> P (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..254
FT /note="IHENSGK -> VPRNLGQ (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> P (in Ref. 1; AAA26140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32113 MW; 43D40C239CDDE307 CRC64;
MGKLRQIAFY GKGGIGKSTT SQNTLAALVE MGQKILIVGC DPKADSTRLI LNTKLQDTVL
HLAAEAGSVE DLEVEDVVKI GYKGIKCTEA GGPEPGVGCA GRGVITAINF LEENGAYDDV
DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYANSGGVRL
GGLICNERKT DRELELAEAL AAKLGCKMIH FVPRNNVVQH AELRRETVIQ YDPTCSQAQE
YRELARKIHE NSGKGVIPTP ITMEELEEML MDFGIMQSEE DREKQIAEME AAMKA
