ID F6D761_METPW Unreviewed; 493 AA.
AC F6D761;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN OrderedLocusNames=MSWAN_2011 {ECO:0000313|EMBL:AEG19020.1};
OS Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=868131 {ECO:0000313|EMBL:AEG19020.1, ECO:0000313|Proteomes:UP000009231};
RN [1] {ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. SWAN-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG19020.1, ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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}.
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DR EMBL; CP002772; AEG19020.1; -; Genomic_DNA.
DR RefSeq; WP_013826519.1; NC_015574.1.
DR AlphaFoldDB; F6D761; -.
DR SMR; F6D761; -.
DR STRING; 868131.MSWAN_2011; -.
DR GeneID; 10669529; -.
DR KEGG; mew:MSWAN_2011; -.
DR eggNOG; arCOG00598; Archaea.
DR HOGENOM; CLU_025876_1_0_2; -.
DR OrthoDB; 72973at2157; -.
DR Proteomes; UP000009231; Chromosome.
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; 3.40.50.12380; Nitrogenase MoFe cofactor biosynthesis protein NifE, C-terminal; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 1.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005974; Nase_asu.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR NCBIfam; TIGR01284; alt_nitrog_alph; 1.
DR NCBIfam; TIGR01862; N2-ase-Ialpha; 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; PS00090; NITROGENASE_1_2; 1.
PE 4: Predicted;
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};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004022}.
FT DOMAIN 48..454
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT REGION 470..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 55257 MW; 07E82CBC87A24D92 CRC64;
MPYKLFDADK EIPEREKHVY KKHCSDPDGE MPHCNTKTVP GSMTERGCAF AGAKGVITGA
LKDVLHVVHS PVGCTTYSAG TKRYPTSPDL PDGTKFPIEN FNLKYVCGTD IQESDVVFGG
MKRLKRSIIE ASKEFPEANA IYTYATCTTG LIGDDMDAVA KELTEELGKD VVAFNAPGFA
GPSQSKGHHI ANHTIFDRLV GTKEPPNTTP YDVGLIGEYN IDGDLWVLES YFKEMGIRIL
SRFSGDSTHD ELCWMHRPKL NLVRCQRSAT YIADLIKDKY DVPYIKVDFF STEYCAENLR
TIGKYFGLEK EAEKVIADRM AKVGPELEFY KKKLQGKKVY IFSGGPKSWH LAIPLENELG
MDVTAVASQF EHEDGYVKMK KRVDEGVLIV DDPNSLEFEE MIEEDKPDLI LAGIKEKYLA
HKLGVPSIMI HSYENGPYIG FEGFLNLAKD MYANIYNPVW NLVEFEENPA GEEESKIESG
SIEKEDNQVE VAK
//
