ID   NIFD_CROS5              Reviewed;         480 AA.
AC   O07642; A1KYD6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=cce_0560;
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10594374; DOI=10.1016/s0304-4165(99)00196-8;
RA   Colon-Lopez M.S., Tang H.-Y., Tucker D.L., Sherman L.A.;
RT   "Analysis of the nifHDK operon and structure of the NifH protein from the
RT   unicellular, diazotrophic cyanobacterium, Cyanothece strain sp. ATCC
RT   51142.";
RL   Biochim. Biophys. Acta 1473:363-375(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18226230; DOI=10.1186/1471-2148-8-30;
RA   Kneip C., Voss C., Lockhart P.J., Maier U.G.;
RT   "The cyanobacterial endosymbiont of the unicellular algae Rhopalodia gibba
RT   shows reductive genome evolution.";
RL   BMC Evol. Biol. 8:30-30(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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; AF003337; AAB61283.1; -; Genomic_DNA.
DR   EMBL; AY728386; AAW56989.1; -; Genomic_DNA.
DR   EMBL; CP000806; ACB49911.1; -; Genomic_DNA.
DR   RefSeq; WP_009546640.1; NC_010546.1.
DR   AlphaFoldDB; O07642; -.
DR   SMR; O07642; -.
DR   STRING; 43989.cce_0560; -.
DR   EnsemblBacteria; ACB49911; ACB49911; cce_0560.
DR   KEGG; cyt:cce_0560; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025876_1_1_3; -.
DR   OMA; CGQYSWA; -.
DR   OrthoDB; 363662at2; -.
DR   Proteomes; UP000001203; Chromosome circular.
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..480
FT                   /note="Nitrogenase molybdenum-iron protein alpha chain"
FT                   /id="PRO_0000153065"
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         274
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /evidence="ECO:0000250"
FT   BINDING         441
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   480 AA;  53682 MW;  3D83D095EC405E05 CRC64;
     MATVEDNKKL IADVLSTYPE KAAKKRAKHL GVYEEGEADC GVKSNKQSLP GVMTARGCAY
     AGSKGVVWGP IKDMVHISHG PVGCGYYSWS GRRNYYIGTT GVDSFGTMQF TSDFQERDIV
     FGGDKKLAKI IDEIEELFPL NGGVSVQSEC PVGLIGDDIE SVARTKSKET GKSVVPVRCE
     GFRGVSQSLG HHIANDMIRD WVFPTADKEN AEKGFEGTPY DVAIIGDYNI GGDAWSSRIL
     LEEIGLRVVA QWSGDGTLTE MKATPNVKLN LIHCYRSMNY ISRHMEEKYG IPWLEYNFFG
     PSKIAASLRE IASRFDEKIQ AKAEEVIEKY RKQSEEIIAK YRPRLEGKTV MMMVGGLRPR
     HVVPAFKDLG MEIIGTGYEF AHGDDYKRTT GYVEDATLIY DDVTGYEFEE FVKELKPDLV
     AAGIKEKYVF QKMALPFRQM HSWDYSGPYH GYDGFAIFAR DMDLALNSPT WGLIGTPWNK