ID A0A0X8CMM3_9BRAD Unreviewed; 518 AA.
AC A0A0X8CMM3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=FeMo cofactor biosynthesis protein NifB {ECO:0000256|ARBA:ARBA00021702};
DE AltName: Full=Nitrogenase cofactor maturase NifB {ECO:0000256|ARBA:ARBA00032102};
DE AltName: Full=Radical SAM assemblase NifB {ECO:0000256|ARBA:ARBA00030926};
GN ORFNames=BCCGELA001_31090 {ECO:0000313|EMBL:AMA60227.1};
OS Bradyrhizobium sp. CCGE-LA001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA60227.1, ECO:0000313|Proteomes:UP000019052};
RN [1] {ECO:0000313|EMBL:AMA60227.1, ECO:0000313|Proteomes:UP000019052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA60227.1,
RC ECO:0000313|Proteomes:UP000019052};
RX PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT related Phaseolus species.";
RL Mol. Phylogenet. Evol. 79:1-11(2014).
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:0000256|ARBA:ARBA00003522}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005155}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. NifB family.
CC {ECO:0000256|ARBA:ARBA00006804}.
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DR EMBL; CP013949; AMA60227.1; -; Genomic_DNA.
DR RefSeq; WP_008545825.1; NZ_CP013949.1.
DR AlphaFoldDB; A0A0X8CMM3; -.
DR STRING; 1223566.BCCGELA001_31090; -.
DR KEGG; brc:BCCGELA001_31090; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000019052; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; SFLDS00029; Radical_SAM; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 68..317
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 518 AA; 56816 MW; 2F29D5FBFE8409DE CRC64;
MNAVAGRGKN VKAAEAGGKM RVIGDQKACR SQSRDGTASC GLQPVQGGVS SEIWKKIKNH
PCYSEEAHHH YARMHVAVAP ACNIQCNYCN RKYDCANESR PGVVSEKLTP EQAARKLVAV
AASIPQLSVI GIAGPGDSLA NPRKTFKTFE LIAAAAPDIK LCLSTNGLDL PDHVDTISRC
KIDHVTITIN MIDPEIGARI YPWIFFNHKR YTGTEASKIL TSRQLKGLEM LSERGVLCKI
NSVMIPGIND QHLIEVNRAV KSRGAFVHNI MPLISSPEHG TAFGLNGQRG PTAHELKALQ
DACEGQINMM RHCRQCRADA IGLLGDDRSH EFTAEKIMAM HVENELETRK AYHAKIEDER
EAKISARQEE LEKIAGETSE IKLLAAVATK GSGLINEHFG HAREFLVYEL STSAVKFVGH
RRVDLYCQGG YGEEDRLASI IRAINDCHAV FVAKIGGCPR KSLISAGIEP VEQYAHEFIE
TSTIAWFRSY LDKVKSGEIQ HVQRGDAAIR QGPLVSAV
//