ID Q8GPM3_CHLFR Unreviewed; 491 AA.
AC Q8GPM3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
OS Chlorogloeopsis fritschii.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=1124 {ECO:0000313|EMBL:AAN63671.1};
RN [1] {ECO:0000313|EMBL:AAN63671.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 6718 {ECO:0000313|EMBL:AAN63671.1};
RX PubMed=12177735; DOI=10.1007/s00284-001-0111-8;
RA Henson B.J., Watson L.E., Barnum S.R.;
RT "Molecular differentiation of the heterocystous cyanobacteria, Nostoc and
RT Anabaena, based on complete NifD sequences.";
RL Curr. Microbiol. 45:161-164(2002).
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; AF442510; AAN63671.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GPM3; -.
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 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}.
FT DOMAIN 64..473
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 491 AA; 55208 MW; 32595312CF98B4EF CRC64;
MTPPENKNIV EEHKELIKEV LQAYPEKSRK KREKHLNVHE EGKADCGVKS NIKSVPGVMT
ARGCAYAGSK GVVWGPIKDM IHISHGPVGC GYWSWSGRRN YYVGVTGVDS FGTMHFTSDF
QERDIVFGGD KKLTKLIEEI EELFPLNRGI SIQSECPIGL IGDDIEAVAK KSAKQIGKPV
VPLRCEGFRG VSQSLGHHIA NDAIRDWIFP QFDKAKKENK IDFEPGPYDV ALIGDYNIGG
DAWASRMLLE EMGLRVVAQW SGDGTLNELI QGPAAKLVLI HCYRSMNYIC RSLEEAYGMP
WMEFNFFGPT KIAASLREIA AKFDSKIQEN AEKVIAKYTS AMNAIVEKYR PRLEGNTVML
YVGGLRPRHV VPAFEDLGIK VIGTGYEFAH NDDYKRTTHY IDNATIIYDD VTAYEFEEFV
KAKKPDLIAS GIKEKYVFQK MGLPFRQMHS WDYSGPYHGY DGFAIFARDM DLALNSPTWS
LVGCSLEKVR S
//
