(data stored in ACNUC7421 zone)

HOGENOM: DENA2_1_PE1015

ID   DENA2_1_PE1015                       STANDARD;      PRT;   290 AA.
AC   DENA2_1_PE1015; D4H6V6;
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; (DENA2_1.PE1015).
GN   Name=nifH; OrderedLocusNames=Dacet_1046;
OS   DENITROVIBRIO ACETIPHILUS DSM 12809.
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Denitrovibrio.
OX   NCBI_TaxID=522772;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DENA2_1.PE1015.
CC       Denitrovibrio acetiphilus DSM 12809 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D4H6V6_DENA2
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-101 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; D4H6V6; -.
DR   EMBL; CP001968; ADD67822.1; -; Genomic_DNA.
DR   RefSeq; YP_003503778.1; NC_013943.1.
DR   ProteinModelPortal; D4H6V6; -.
DR   GeneID; 8875395; -.
DR   GenomeReviews; CP001968_GR; Dacet_1046.
DR   KEGG; dap:Dacet_1046; -.
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:HAMAP.
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:HAMAP.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:HAMAP.
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; DENA2_1.PE1015; -.
KW   4Fe-4S; ADP-ribosylation; ATP-binding; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW   Oxidoreductase.
SQ   SEQUENCE   290 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MALRQIAFYG KGGIGKSTTS QNTLAAMAEM GKKIMIVGCD PKADSTRLIL HSKAQSTIME
     LAAEAGSVED LELDDVLKAG YLDIRCVEAG GPEPGVGCAG RGVITAINFL EEEGAYEEDL
     DFVSYDVLGD VVCGGFAMPI REGKAQEIYI VTSGEMMAMY AANNISKGIL KYANSGGVRL
     AGLICNERQT DREDELISEL ASKINTQMIH FVPRDNIVQH AELRRMTVVE YDGKCKQADE
     YRTLANKIIN NKMFNIPTPV SMQELEDLLM EFGIITEDDE AIVGKKAHEA
//

If you have problems or comments...

PBIL Back to PBIL home page