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Database: UniProt
Entry: Q8KLB8_RHIEC
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Original site: Q8KLB8_RHIEC 
ID   Q8KLB8_RHIEC            Unreviewed;       492 AA.
AC   Q8KLB8;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 138.
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   OrderedLocusNames=RHE_PD00229 {ECO:0000313|EMBL:AAM54822.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid sym p42d {ECO:0000313|Proteomes:UP000001936}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:AAM54822.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=12801410; DOI=10.1186/gb-2003-4-6-r36;
RA   Gonzalez V., Bustos P., Ramirez-Romero M.A., Medrano-Soto A., Salgado H.,
RA   Hernandez-Gonzalez I., Hernandez-Celis J.C., Quintero V.,
RA   Moreno-Hagelsieb G., Girard L., Rodriguez O., Flores M., Cevallos M.A.,
RA   Collado-Vides J., Romero D., Davila G.;
RT   "The mosaic structure of the symbiotic plasmid of Rhizobium etli CFN42 and
RT   its relation to other symbiotic genome compartments.";
RL   Genome Biol. 4:R36.1-R36.13(2003).
RN   [2] {ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; U80928; AAM54822.1; -; Genomic_DNA.
DR   RefSeq; WP_011053432.1; NC_004041.2.
DR   AlphaFoldDB; Q8KLB8; -.
DR   KEGG; ret:RHE_PD00229; -.
DR   HOGENOM; CLU_027639_0_0_5; -.
DR   OrthoDB; 9785734at2; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000001936; Plasmid sym p42d.
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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Plasmid {ECO:0000313|EMBL:AAM54822.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          62..311
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   492 AA;  53635 MW;  927BB3F2455E2C5B CRC64;
     MSAPMISLES ATSTTSLDQL LATAKPSGCT SSSCGVSTKP ADVDQAIWAK IKNHPCYSEE
     AHHYFARMHV AVAPACNIQC NYCNRKYDCA NESRPGVVSE KLTPDQALRK VIAVANEVPQ
     LSVLGVAGPG DACYDWKKTK ETFERVAGEI HDIKLCISTN GLALPDHVAE LVDMNVDHVT
     ITINMVDPEI GAKIYPWIFY RNRRYTGIEA ARILHERQMV GLEMLTACGI ITKVNSVMIP
     GVNDEHLVEV NKWVKERGAF LHNVMPLISD PAHGTYYGLT GQRGPRALEL KALQDRLEGG
     AKLMRHCRQC RADAVGLLGD DRGQEFALDQ LPGEITYDAR KREAYREVIA RERGDHATAK
     SEAIETVKAA GDGSLHVAVA TKGGGRINEH FGHAKEFQVY EASSRGITYV GHRKIEQYCL
     GGRGEEATLD GIITALVGID VVLCAKIGEC PKTKLMEAGV RATDAYCYDY IETAIGTLYA
     AKFGVEPQAA TA
//
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