位置:首页 > 蛋白库 > NIFB_NOSS1
NIFB_NOSS1
ID   NIFB_NOSS1              Reviewed;         475 AA.
AC   P20627;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 127.
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; OrderedLocusNames=all1517;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2553733; DOI=10.1016/s0021-9258(19)47287-6;
RA   Mulligan M.E., Haselkorn R.;
RT   "Nitrogen fixation (nif) genes of the cyanobacterium Anabaena species
RT   strain PCC 7120. The nifB-fdxN-nifS-nifU operon.";
RL   J. Biol. Chem. 264:19200-19207(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J05111; AAA22004.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77883.1; -; Genomic_DNA.
DR   PIR; AG1995; AG1995.
DR   RefSeq; WP_010995686.1; NZ_RSCN01000022.1.
DR   AlphaFoldDB; P20627; -.
DR   SMR; P20627; -.
DR   STRING; 103690.17135337; -.
DR   PRIDE; P20627; -.
DR   EnsemblBacteria; BAB77883; BAB77883; BAB77883.
DR   KEGG; ana:all1517; -.
DR   eggNOG; COG0535; Bacteria.
DR   eggNOG; COG1433; Bacteria.
DR   OMA; NHPCYSE; -.
DR   OrthoDB; 1199289at2; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000002483; Chromosome.
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: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; 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   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   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..475
FT                   /note="FeMo cofactor biosynthesis protein NifB"
FT                   /id="PRO_0000153035"
FT   DOMAIN          52..303
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         66
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         70
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         72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         73
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         120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         172
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   475 AA;  52876 MW;  29339C51D55E25E9 CRC64;
     MTPPVTGSSV TESTPTKAKS GGCGCDTSTT VEMDEKLQER IAKHPCYSEE AHHHYARMHV
     AVAPACNIQC NYCNRKYDCA NESRPGVVSE LLTPEEAAHK VLVIAGKIPQ MTVLGIAGPG
     DPLANPEKTF RTFELIADKA PDIKLCLSTN GLMLPEYVDR IKQLNIDHVT ITLNTIDPEI
     GAQIYSWVHY KRRRYRGAEG ARILLEKQME GLQALREADI LCKVNSVMIP GINDQHLVEV
     NKMIREQGAF LHNIMPLISA PEHGTHFGLT GQRGPSQKEL KSVQDQCSGN MKMMRHCRQC
     RADAVGLLGE DRSQEFTKDK FLEMAPEYDF DKRQEVHEGI EKFRVELKVA KEKVLAGKEK
     TANNPKILVA IATKGGGLVN QHFGHAKEFQ VYEVDGSEVS FVSHRKVDHY CQGGYGEEAT
     FDNIVKTIAD CKAVLVSKIG ESPKEKLLQA GIQTVEAYDV IEKVALEFYE QWNKG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024