NIFB_RHILT
ID NIFB_RHILT Reviewed; 490 AA.
AC P24427;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 98.
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 Rhizobium leguminosarum bv. trifolii.
OG Plasmid sym pRtr843e.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=386;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ANU 843;
RX PubMed=2622339; DOI=10.1111/j.1365-2958.1989.tb00161.x;
RA Iismaa S.E., Ealing P.M., Scott K.F., Watson J.M.;
RT "Molecular linkage of the nif/fix and nod gene regions in Rhizobium
RT leguminosarum biovar trifolii.";
RL Mol. Microbiol. 3:1753-1764(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-153.
RC STRAIN=ANU 843;
RX PubMed=2552256; DOI=10.1111/j.1365-2958.1989.tb00244.x;
RA Watson J.M., Iismaa S.E.;
RT "The nifA gene product from Rhizobium leguminosarum biovar trifolii lacks
RT the N-terminal domain found in other NifA proteins.";
RL Mol. Microbiol. 3:943-955(1989).
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; X51963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X16311; CAA34378.1; -; Genomic_DNA.
DR PIR; S09279; S09279.
DR AlphaFoldDB; P24427; -.
DR SMR; P24427; -.
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: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 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 Plasmid; S-adenosyl-L-methionine.
FT CHAIN 1..490
FT /note="FeMo cofactor biosynthesis protein NifB"
FT /id="PRO_0000153044"
FT DOMAIN 60..309
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
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 78
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="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 81
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 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 305
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
SQ SEQUENCE 490 AA; 53926 MW; B366183E6AF5CF5B CRC64;
MSRGMSKCRI TNTAPSARGW KATTFGDYAF SSRGSSEPNA MAPAIIEQIK DHPCFSREAH
LYFARMHLAV ASACNIQCNY CNRKYDCANE SRPGVASHRL TPDQALRRAI AVANEVPQLS
VVGIAGPGDA CYDWRKTKAT LIPIAREIPD VKLCISTNGL ALPEHVDDLV DMNVGHVTIT
INMVDPRIGT KIYPWIFYDG RRYNGIDASR ILHERQMLGL EMLTERGILA KVNSVMIPGV
NDEHLIEVNK WVKDRGAFMH NVMPLISERS HGTFYGLNDQ RCPATSELIA LRDRLEGGTQ
VMRHCHQCRA DAVGLLGDDR AREFTLGQFP ADETYDSAKR NAYRQLIERE RRGQTLEESD
AATPVSAPSD ELLLIAVTTK GGGRVNGHFG HAQEIQIFSV CQKGNGLIGH LKIDPYCLGG
WGEEATLNTI IDALKGLDVL ICSEIGKSPK NKLARRGVRA TGAYDGSYIE QAIGALYRAV
LHNEALATAI
