NIFD_RIPO1
ID NIFD_RIPO1 Reviewed; 476 AA.
AC Q55029; B7JWY3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Nitrogenase molybdenum-iron protein alpha chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase;
DE AltName: Full=Nitrogenase component I;
GN Name=nifD; OrderedLocusNames=PCC8801_1786;
OS Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen H.M.;
RT "Synechococcus RF-1 nifHDK sequences.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC complex that catalyzes the key enzymatic reactions in nitrogen
CC fixation.
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=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Evidence={ECO:0000250};
CC Note=Binds 1 [8Fe-7S] cluster per heterodimer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC Evidence={ECO:0000250};
CC Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; U22146; AAA64844.1; -; Genomic_DNA.
DR EMBL; CP001287; ACK65832.1; -; Genomic_DNA.
DR RefSeq; WP_012595105.1; NC_011726.1.
DR AlphaFoldDB; Q55029; -.
DR SMR; Q55029; -.
DR STRING; 41431.PCC8801_1786; -.
DR EnsemblBacteria; ACK65832; ACK65832; PCC8801_1786.
DR KEGG; cyp:PCC8801_1786; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_1_1_3; -.
DR OMA; CGQYSWA; -.
DR OrthoDB; 363662at2; -.
DR Proteomes; UP000008204; Chromosome.
DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; cd01976; Nitrogenase_MoFe_alpha; 1.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005972; Nase_Mo-Fe_asu.
DR PANTHER; PTHR43457; PTHR43457; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR TIGRFAMs; TIGR01282; nifD; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..476
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153083"
FT BINDING 58
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT CONFLICT 141
FT /note="N -> H (in Ref. 1; AAA64844)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..177
FT /note="IPV -> FPF (in Ref. 1; AAA64844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53742 MW; 1B02C62EE0C59D06 CRC64;
MSTVEDRKQL IQDVLDTYPE KLAKKRSKHL NVYEEGKDDC GVKSNIKSAP GVMTARGCAY
AGSKGVVWGP IKDMIHISHG PVGCGYYSWS GRRNYYIGTT GVDTFGTMNF TSDFQEKDIV
FGGDKKLLKI TEEIEELFPL NNGISIQSEC PVGLIGDDIE GVAKKAQKIT GKPVIPVRCE
GFRGVSQSLG HHIANDAVRD WVFSRDDAQE IETTPYDVAI IGDYNIGGDA WSSRILLEEM
GLRVVAQWSG DGTINEMMQT PKVKLNLIHC YRSMNYISRH MEEKYGIPWF EYNFFGPTKI
AESLRAIAAL FDDTIKENAE KVIAKYEQQT AEVLAKYRPR LENKTVMMMV GGLRPRHVVP
AFTDLGMKMI GTGYEFAHGD DYKRTTEYVD DATLIYDDVT AYEFEKFVQE LKPDLVASGV
KEKYVFQKMG LPFRQMHSWD YSGPYHGYDG FAIFARDMDL ALNNPTWGLI KSPWNK
