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VNFD_AZOCH
ID   VNFD_AZOCH              Reviewed;         473 AA.
AC   P15332;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Nitrogenase vanadium-iron protein alpha chain;
DE            EC=1.18.6.1;
DE   AltName: Full=Dinitrogenase 2 subunit alpha;
DE   AltName: Full=Nitrogenase component I;
GN   Name=vnfD;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2388847; DOI=10.1093/nar/18.15.4616;
RA   Fallik E., Robson R.L.;
RT   "Completed sequence of the region encoding the structural genes for the
RT   vanadium nitrogenase of Azotobacter chroococcum.";
RL   Nucleic Acids Res. 18:4616-4616(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX   PubMed=2743980; DOI=10.1002/j.1460-2075.1989.tb03495.x;
RA   Robson R.L., Woodley P.R., Pau R.N., Eady R.R.;
RT   "Structural genes for the vanadium nitrogenase from Azotobacter
RT   chroococcum.";
RL   EMBO J. 8:1217-1224(1989).
CC   -!- FUNCTION: This vanadium-iron protein is part of the nitrogenase complex
CC       that catalyzes the key enzymatic reactions in nitrogen fixation.
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   -!- COFACTOR:
CC       Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Evidence={ECO:0000250};
CC       Note=Binds 1 [8Fe-7S] cluster per heterodimer. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[7Fe-V-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:60357;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [7Fe-V-9S-C-homocitryl] cluster per subunit.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC   -!- MISCELLANEOUS: The structure of the 7Fe-V-9S-C-homocitryl cluster is
CC       assumed to be analogous to the 7Fe-Mo-9S-C-homocitryl cluster.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; X51756; CAA36058.1; -; Genomic_DNA.
DR   EMBL; X15077; CAA33173.1; -; Genomic_DNA.
DR   PIR; S04113; S04113.
DR   AlphaFoldDB; P15332; -.
DR   SMR; P15332; -.
DR   BRENDA; 1.18.6.2; 617.
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:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051212; F:vanadium ion binding; IEA:InterPro.
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   InterPro; IPR010142; Nase_V-Fe_asu.
DR   PANTHER; PTHR43457; PTHR43457; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR   TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR   TIGRFAMs; TIGR01860; VNFD; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Vanadium.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2743980"
FT   CHAIN           2..473
FT                   /note="Nitrogenase vanadium-iron protein alpha chain"
FT                   /id="PRO_0000153055"
FT   BINDING         49
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with beta chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with beta chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with beta chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="[7Fe-V-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:60357"
FT                   /evidence="ECO:0000250"
FT   BINDING         422
FT                   /ligand="[7Fe-V-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:60357"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        50..53
FT                   /note="LLRR -> AFCGA (in Ref. 1; CAA36058)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  53993 MW;  2C1CE3FB8C6AEAED CRC64;
     MPMVLLECDK DIPERQKHIY LKAPNEDTRE FLPIANAATI PGTLSERGCL LRRKLVIGGV
     LKDTIQMIHG PLGCAYDTWH TKRYPTDNGH FNMKYVWSTD MKESHVVFGG EKRLEQRMHE
     AFDEMPDIKR MIVYTTCPTA LIGDDIKAVA KKVMKERPDV DVFTVECPGF SGVSQSKGHH
     VLNIGWINEK VETMEKEITS EYTMNFIGDF NIQGDTQLLQ TYWDRLGIQV VAHFTGNGTY
     DDLRCMHQAQ LNVVNCARSS GYIANELKKR YGIPRLDIDS WGFSYMAEGI RKICAFFGIE
     EKGERLIAEE YAKWKPKLDW YKERLQGKKM AIWTGGPRLW HWTKSVEDDL GIQVVAMSSK
     FGHEEDFEKV IARGKEGTYY IDDGNELEFF EIIDLVKPDV IFTGPRVGEL VKKLHIPYVN
     GHGYHNGPYM GFEGFVNLAR DTYNAVHNPL RHLAAVDIRD SSQTTPVIVR GAA
 
 
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