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Database: UniProt/SWISS-PROT
Entry: NIFD_METTH
LinkDB: NIFD_METTH
Original site: NIFD_METTH 
ID   NIFD_METTH              Reviewed;         469 AA.
AC   O27605;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   19-FEB-2014, entry version 90.
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=MTH_1563;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /
OS   JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP
CC       + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16
CC       phosphate.
CC   -!- COFACTOR: Binds 1 8Fe-7S cluster per heterodimer (By similarity).
CC   -!- COFACTOR: Binds 1 7Fe-Mo-9S-C-homocitryl cluster per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex
CC       with the iron protein (nitrogenase component 2).
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
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DR   EMBL; AE000666; AAB86037.1; -; Genomic_DNA.
DR   PIR; F69075; F69075.
DR   RefSeq; NP_276676.1; NC_000916.1.
DR   ProteinModelPortal; O27605; -.
DR   STRING; 187420.MTH1563; -.
DR   EnsemblBacteria; AAB86037; AAB86037; MTH_1563.
DR   GeneID; 1471832; -.
DR   KEGG; mth:MTH1563; -.
DR   eggNOG; COG2710; -.
DR   KO; K02586; -.
DR   OMA; KCIPERK; -.
DR   ProtClustDB; CLSK878514; -.
DR   BioCyc; MTHE187420:GJNM-1565-MONOMER; -.
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   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR005974; Nase_asu.
DR   InterPro; IPR010143; Nase_comp1_asu.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR   TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Molybdenum; Nitrogen fixation; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    469       Nitrogenase molybdenum-iron protein alpha
FT                                chain.
FT                                /FTId=PRO_0000153073.
FT   METAL        48     48       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL        74     74       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL       147    147       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL       265    265       Molybdenum-iron-sulfur-carbon (7Fe-Mo-9S-
FT                                C-homocitryl) (By similarity).
FT   METAL       431    431       Molybdenum-iron-sulfur-carbon (7Fe-Mo-9S-
FT                                C-homocitryl); via pros nitrogen (By
FT                                similarity).
SQ   SEQUENCE   469 AA;  52866 MW;  7D2CD5FFED9EC7B8 CRC64;
     MPFKLFDVDA EIPERKKHVY IKKKEDPEED LPLCNTKTIP GCMTERGCAF AGAKGVITGA
     IKDALHVIHS PVGCTAYGYG TKRYPTSQEM PDGSLFPIEN FNLKYITGTN LTETDVVFGG
     MDKLKRCIIE AAKEFPEANA VYTYATCTTG LIGDDIEAVS REVSEEIGKD VVAINAPGFA
     GPTQSKGHQV ANYTLFENLV GTAEPPVVTD YDVNLIGEYN IDGDLWVLKR YFEEMGINVL
     STFTGDCCHD EIKWMHRAKL SLVRCQRSAT YIARLLEERY NVPYMKVDFF GIEYCKRNLM
     ATGEYFGIPE RAEEVIKDRM EKIGPEIEYL RNKLAGKKVW VFSGGPKNWH LPRPLEDELG
     MEVVAVSTMF EHEDGYEKIK KRVGENTVIV DDPNSLELEE IIEKYRPDII LSGIKEKYLA
     HKLGVPCVLI HSYENGPYIG FEGFLNLARD MYASIYSPVW DLLEFEAGD
//
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