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NIFB_AZOVI
ID   NIFB_AZOVI              Reviewed;         502 AA.
AC   P11067;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=FeMo cofactor biosynthesis protein NifB;
DE            EC=4.-.-.-;
DE   AltName: Full=Nitrogenase cofactor maturase NifB;
DE   AltName: Full=Radical SAM assemblase NifB;
GN   Name=nifB;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2450865; DOI=10.1128/jb.170.4.1475-1487.1988;
RA   Joerger R.D., Bishop P.E.;
RT   "Nucleotide sequence and genetic analysis of the nifB-nifQ region from
RT   Azotobacter vinelandii.";
RL   J. Bacteriol. 170:1475-1487(1988).
CC   -!- FUNCTION: Involved in the biosynthesis of the iron-molybdenum cofactor
CC       (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the
CC       nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes
CC       the crucial step of radical SAM-dependent carbide insertion that occurs
CC       concomitant with the insertion of a 9th sulfur and the
CC       rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C]
CC       cluster, the precursor to the M-cluster.
CC       {ECO:0000250|UniProtKB:D5VRM1}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:D5VRM1};
CC       Note=Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two
CC       others probably act as substrate. {ECO:0000250|UniProtKB:D5VRM1};
CC   -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC       {ECO:0000250|UniProtKB:D5VRM1}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. NifB family.
CC       {ECO:0000305}.
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DR   EMBL; J03411; AAA22148.1; -; Genomic_DNA.
DR   PIR; B27733; B27733.
DR   AlphaFoldDB; P11067; -.
DR   SMR; P11067; -.
DR   DIP; DIP-61142N; -.
DR   BioCyc; MetaCyc:MON-19485; -.
DR   UniPathway; UPA00782; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:CACAO.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd00852; NifB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.420.130; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR003731; Di-Nase_FeMo-co_biosynth.
DR   InterPro; IPR036105; DiNase_FeMo-co_biosyn_sf.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR005980; Nase_CF_NifB.
DR   InterPro; IPR034165; NifB_C.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR43787:SF3; PTHR43787:SF3; 1.
DR   Pfam; PF02579; Nitro_FeMo-Co; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF53146; SSF53146; 1.
DR   TIGRFAMs; TIGR01290; nifB; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Nitrogen fixation;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..502
FT                   /note="FeMo cofactor biosynthesis protein NifB"
FT                   /id="PRO_0000153036"
FT   DOMAIN          53..301
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         297
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT   BINDING         300
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
SQ   SEQUENCE   502 AA;  54579 MW;  C0CFDE71DE1429D1 CRC64;
     MELSVLGQNN GGQHSAGGCS SSSCGSTHDQ LSHLPENIRA KVQNHPCYSE EAHHYFARMH
     VAVAPACNIQ CHYCNRKYDC ANESRPGVVS EVLTPEQAVK KVKAVAAAIP QMSVLGIAGP
     GDPLANPKRT LDTFRMLSEQ APDMKLCVST NGLALPECVE ELAKHNIDHV TITINCVDPE
     IGAKIYPDLL EQQAHPRRQG RKILIEQQQK GLEMLVARGI LVKVNSVMIP GVNDEHLKEV
     SKIVKAKGAF LHNVMPLIAE PEHGTFYGVM GQRSPEPEEL QDLQDACAGD MNMMRHCRQC
     RADAVGMLGE DRGDEFTLDK IESMEIDYEA AMVKRAAIHA AIKEELDEKA AKKERLAGLS
     VASVQNGTSG RYRPVLMAVA TSGGGLINQH FGHATEFLVY EASPSGVRFI GHRRVDQYCV
     GNDTCGEKES ALAGSIRALK GCEAVLCSKI GFEPWSDLET AGIQPNGEHA MEPIEEAVMA
     VYREMIESGR LENDGALLQA KA
 
 
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