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ANFK_RHOCA
ID   ANFK_RHOCA              Reviewed;         460 AA.
AC   Q07935;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Nitrogenase iron-iron protein beta chain;
DE            EC=1.18.6.1;
DE   AltName: Full=Dinitrogenase 3 subunit beta;
DE   AltName: Full=Nitrogenase component I;
GN   Name=anfK;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B10S;
RX   PubMed=8332060; DOI=10.1111/j.1365-2958.1993.tb01611.x;
RA   Schueddekopf K., Hennecke S., Liese U., Kutsche M., Klipp W.;
RT   "Characterization of anf genes specific for the alternative nitrogenase and
RT   identification of nif genes required for both nitrogenases in Rhodobacter
RT   capsulatus.";
RL   Mol. Microbiol. 8:673-684(1993).
CC   -!- FUNCTION: This iron-iron protein is part of the nitrogenase complex
CC       that catalyzes the key enzymatic reactions in nitrogen fixation. Other
CC       nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-
CC       iron protein.
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   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; X70033; CAA49627.1; -; Genomic_DNA.
DR   PIR; S34947; S34947.
DR   AlphaFoldDB; Q07935; -.
DR   SMR; Q07935; -.
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; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR014280; Nase_Fe-Fe_bsu.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR02931; anfK_nitrog; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Iron; Iron-sulfur; Metal-binding; Nitrogen fixation;
KW   Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..460
FT                   /note="Nitrogenase iron-iron protein beta chain"
FT                   /id="PRO_0000153108"
FT   BINDING         20
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  50703 MW;  D20D361C76DAF8D4 CRC64;
     MTCQVTQKAR EGTINPIFTC QPAGAQFASI GIKDCIGIVH GGQGCVMFVR LLISQHMKES
     FEIASSSVHE DGAVFGALDR VETAVEVLLT RYPDVKVVPI ITTCSTEIIG DDVDGLLSKL
     EDELLPTKFP GREVHLLTVH CPSFVGSMIT GYDKAVHDFV KKFATKDEPS DKINLITGWV
     NPGDVKELKH LLEVMEVKAN VLFEVESFDS PLMPDLEHHS HGSTTIEDLR DTANAKGTIA
     LNRYEGMKAA DYLKKKFKVP AVIGPTPVGI RNTDAFLKAV SEMTGQPIPA QLVKERGLAL
     DAIADIGHMF LADKRVAIYA NPDLAIGLTE FCLDLEMKPK LLLLGDDNSG YVKDPRVVAL
     QENAPDLEIV TNADFWDLES RIQQGLELDL ILGHSKGRFI SIDYKVPMVR VGFPTYDRAG
     MYRHPVLGYG GAMFLAETMA NTLFADMEAK KNKEWILNVW
 
 
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