(data stored in ACNUC7421 zone)

HOGENOM: SYNFM_1_PE1009

ID   SYNFM_1_PE1009                       STANDARD;      PRT;   274 AA.
AC   SYNFM_1_PE1009; A0LH11;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Nitrogenase iron protein; EC=1.18.6 1;AltName:
DE   Full=Nitrogenase Fe protein;AltName: Full=Nitrogenase component
DE   II;AltName: Full=Nitrogenase reductase; (SYNFM_1.PE1009).
GN   Name=nifH; OrderedLocusNames=Sfum_1019;
OS   SYNTROPHOBACTER FUMAROXIDANS MPOB.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SYNFM_1.PE1009.
CC       Syntrophobacter fumaroxidans MPOB, complete genome.
CC       1..88329 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:NIFH_SYNFM
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the
CC       iron protein and the molybdenum-iron protein (By similarity).
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 4Fe-4S cluster per dimer (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- PTM: The reversible ADP-ribosylation of Arg-97 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC   -!- GENE_FAMILY: HOG000228826 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A0LH11; -.
DR   EMBL; CP000478; ABK16713.1; -; Genomic_DNA.
DR   RefSeq; YP_845148.1; NC_008554.1.
DR   ProteinModelPortal; A0LH11; -.
DR   SMR; A0LH11; 1-271.
DR   STRING; A0LH11; -.
DR   GeneID; 4460955; -.
DR   GenomeReviews; CP000478_GR; Sfum_1019.
DR   KEGG; sfu:Sfum_1019; -.
DR   NMPDR; fig|335543.6.peg.1059; -.
DR   eggNOG; COG1348; -.
DR   OMA; CTESGGP; -.
DR   ProtClustDB; PRK13235; -.
DR   BioCyc; SFUM335543:SFUM_1019-MON; -.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00533; NifH; 1; -.
DR   InterPro; IPR000392; Nitogenase_NifH/Reductase_ChlL.
DR   InterPro; IPR005977; Nitrogenase_Fe_NifH.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   PRINTS; PR00091; NITROGNASEII.
DR   TIGRFAMs; TIGR01287; NifH; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
DR   HOGENOMDNA; SYNFM_1.PE1009; -.
KW   4Fe-4S; ADP-ribosylation; ATP-binding; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW   Oxidoreductase.
SQ   SEQUENCE   274 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRKIAIYGKG GIGKSTTTQN TVAGLAEMGR KVMVVGCDPK ADSTRLLLGG LSQKTVLDTL
     RTEGEDVELD DIRKVGFSKS ICVESGGPEP GVGCAGRGII TSINLLEQLG AYASTQALDY
     VFYDVLGDVV CGGFAMPIRE GKAREIYIVV SGEMMAMYAA NNICKGIVKF AEAGGVRLGG
     LICNSRKVDN EKEMIEAFAR QLGTQMIHFV PRDNMVQRAE INRKTVIEFD PAHSQADEYR
     SLARKIEDND MHVIPKPMHT DHLEKLLIEH GLAA
//

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