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Entry: A4J8B9_DESRM
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ID   A4J8B9_DESRM            Unreviewed;       539 AA.
AC   A4J8B9;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE            EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN   OrderedLocusNames=Dred_2818 {ECO:0000313|EMBL:ABO51322.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51322.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO51322.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO51322.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC       complex that catalyzes the key enzymatic reactions in nitrogen
CC       fixation. {ECO:0000256|ARBA:ARBA00002621}.
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         ECO:0000256|RuleBase:RU004022};
CC   -!- COFACTOR:
CC       Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC         Evidence={ECO:0000256|ARBA:ARBA00001969};
CC   -!- COFACTOR:
CC       Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC         Evidence={ECO:0000256|ARBA:ARBA00001919};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC       the iron protein (nitrogenase component 2).
CC       {ECO:0000256|ARBA:ARBA00011462}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC       {ECO:0000256|RuleBase:RU004021}.
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DR   EMBL; CP000612; ABO51322.1; -; Genomic_DNA.
DR   RefSeq; WP_011879117.1; NC_009253.1.
DR   AlphaFoldDB; A4J8B9; -.
DR   STRING; 349161.Dred_2818; -.
DR   KEGG; drm:Dred_2818; -.
DR   eggNOG; COG2710; Bacteria.
DR   HOGENOM; CLU_025876_1_1_9; -.
DR   OrthoDB; 9767044at2; -.
DR   Proteomes; UP000001556; 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   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
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   NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR   NCBIfam; TIGR01282; nifD; 1.
DR   PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU004022};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004022}; Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW   ECO:0000256|RuleBase:RU004021};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004022};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT   DOMAIN          55..507
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
SQ   SEQUENCE   539 AA;  60535 MW;  2FF0C7DC2EC5AFE8 CRC64;
     MAIDEKKLEE IFSQYPAKVK RNRKKHIVIR DPEQARQEIE ANTRTVPGII TNRGCAYAGC
     KGVVLGPLKD IVHITHGPIG CGYYSWLTRR NKAVSEDPKK NFLTYCVSTD MQESDIVFGG
     EKKLARMIDD VVEIFKPNAI TVSATCPVGL IGDDLNAVAK AAEEKHGVPV MAFNCEGYKG
     VSQSAGHHIA NNILMDRVIG QGDWEESPGK YPINMLGEYN IGGDSWEVER VLKEIGYTVI
     SVMTGDGSYK DLKNAHVAEL NLVQCHRSIN YIAEMLETKY GTPWLKVNFI GIQSTIDTLR
     NMALYFGDPE LIRKTEEVIA RELAEIEPVI DQYKKICEGK TAFCFVGGSR GHHYQGLFAE
     LGIETVLAGY EFAHRDDYEG REIIPEIKLD ADTKNIPNLQ VEPDQRRFKL KISPERMEEL
     KKQIPLSYYK GMNVEMKEGH VIVDDLNHYE TEEFIKLLKP DIFASGIKDK YIVQKMGIPA
     KQLHSYDYSG PYAGFKGAVK FAEDVAMGFV SPTWNFTTPP WKNKPIIEGT IEEGGCSKC
//
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