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Database: UniProt
Entry: A0A0X8CMM3_9BRAD
LinkDB: A0A0X8CMM3_9BRAD
Original site: A0A0X8CMM3_9BRAD 
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
//
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