ID NIFB_SINFN Reviewed; 493 AA. AC Q53205; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 143. 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=NGR_a01270; ORFNames=y4uM; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OG Plasmid sym pNGR234a. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8796346; DOI=10.1101/gr.6.7.590; RA Freiberg C., Perret X., Broughton W.J., Rosenthal A.; RT "Sequencing the 500-kb GC-rich symbiotic replicon of Rhizobium sp. NGR234 RT using dye terminators and a thermostable 'sequenase': a beginning."; RL Genome Res. 6:590-600(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=9163424; DOI=10.1038/387394a0; RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A., RA Perret X.; RT "Molecular basis of symbiosis between Rhizobium and legumes."; RL Nature 387:394-401(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=19376903; DOI=10.1128/aem.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion RT systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). 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; Z68203; CAA92412.1; -; Genomic_DNA. DR EMBL; U00090; AAB91885.1; -; Genomic_DNA. DR RefSeq; NP_444098.1; NC_000914.2. DR AlphaFoldDB; Q53205; -. DR SMR; Q53205; -. DR KEGG; rhi:NGR_a01270; -. DR PATRIC; fig|394.7.peg.111; -. DR eggNOG; COG0535; Bacteria. DR HOGENOM; CLU_027639_0_0_5; -. DR OrthoDB; 9785734at2; -. DR UniPathway; UPA00782; -. DR Proteomes; UP000001054; Plasmid sym pNGR234a. 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 CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.30.420.130; Dinitrogenase iron-molybdenum cofactor biosynthesis domain; 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 NCBIfam; TIGR01290; nifB; 1. DR PANTHER; PTHR43787:SF3; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB; 1. DR PANTHER; PTHR43787; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB-RELATED; 1. DR Pfam; PF02579; Nitro_FeMo-Co; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDF00281; FeMo_cofactor_biosynthesis_pro; 1. DR SFLD; SFLDG01068; FeMo_cofactor_biosynthesis_pro; 1. DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1. DR SUPFAM; SSF53146; Nitrogenase accessory factor-like; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 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 Plasmid; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1..493 FT /note="FeMo cofactor biosynthesis protein NifB" FT /id="PRO_0000153046" FT DOMAIN 62..311 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 76 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 80 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 82 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P69848" FT BINDING 83 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 130 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P69848" FT BINDING 182 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P69848" FT BINDING 234 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:P69848" FT BINDING 307 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:D5VRM1" FT BINDING 310 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:D5VRM1" SQ SEQUENCE 493 AA; 53507 MW; 6C8F9A8F87E39AC8 CRC64; MSAPIISLES LTNTTSSGQL LTTAKSGGCA SSSCGSSSRP TDMDSATWEK IKDHPCFSEE AHHYFARMHV AVAPACNIQC NYCNRKYDCA NESRPGVVSE KLTPDQALRK VVAVANEVPQ LSVLGIAGPG DACYDWNKTR ATFERVASEI PDIKLCISTN GLALPEHVDK LAEMNVSHVT ITINMVDPAV GEKIYPWIFY GHRRYTGVDA AKILHEQQML GLEMLTARGI LTKINSVMIP GVNDLHLIEV NKWVKERGAF LHNVMPLISD PAHGTSFGLT GQRGPNALEL KALHDRLEGG AKLMRHCRQC RADAVGLLGT DRGQEFTLDH VPLEPHYDGA KRQAYREVVA RIRDDHLEAK EKAIATVASA NIRGSLQVAV ATKGGGRINE HFGHAKEFQV YEASQTGIKF VGHRKVEPYC HGGWGEDAAL AGIIAALDGI DIVLCARIGD CPKERLMEAG IRATDTYGYD YIEAAISALH ATEFGTAPSQ ATA //