NIFB_METJA
ID NIFB_METJA Reviewed; 300 AA.
AC Q58493;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=FeMo cofactor biosynthesis protein NifB {ECO:0000250|UniProtKB:D5VRM1};
DE EC=4.-.-.-;
DE AltName: Full=Nitrogenase cofactor maturase NifB;
DE AltName: Full=Radical SAM assemblase NifB;
GN Name=nifB {ECO:0000250|UniProtKB:D5VRM1}; OrderedLocusNames=MJ1093;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:D5VRM1}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. NifB family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99096.1; -; Genomic_DNA.
DR PIR; D64436; D64436.
DR RefSeq; WP_010870605.1; NC_000909.1.
DR AlphaFoldDB; Q58493; -.
DR SMR; Q58493; -.
DR STRING; 243232.MJ_1093; -.
DR EnsemblBacteria; AAB99096; AAB99096; MJ_1093.
DR GeneID; 1451989; -.
DR KEGG; mja:MJ_1093; -.
DR eggNOG; arCOG00956; Archaea.
DR HOGENOM; CLU_027639_1_0_2; -.
DR InParanoid; Q58493; -.
DR OMA; PCYNEKL; -.
DR OrthoDB; 46264at2157; -.
DR PhylomeDB; Q58493; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000000805; Chromosome.
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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR005980; Nase_CF_NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43787:SF3; PTHR43787:SF3; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Nitrogen fixation;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..300
FT /note="FeMo cofactor biosynthesis protein NifB"
FT /id="PRO_0000153050"
FT DOMAIN 24..266
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 38
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:D5VRM1,
FT ECO:0000250|UniProtKB:P69848"
FT BINDING 42
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:D5VRM1,
FT ECO:0000250|UniProtKB:P69848"
FT BINDING 45
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:D5VRM1,
FT ECO:0000250|UniProtKB:P69848"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 262
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT BINDING 265
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
SQ SEQUENCE 300 AA; 34568 MW; 5EEA1B14CA4CF1E0 CRC64;
MDKNKMSKFA HITKVHPCFN EKIHDKVGRV HLPVAPRCNI ACKFCRRSLG KEACEHRPGV
ALSVLKPEDV ESYLNKVLKE IPNIKVVGIA GPGDSLFNKE TFETLKIIDE KFPNLIKCLS
TNGLLLNKYY KKLADLNVKT VTVTVNAIDP EILKEIVEWV YYDKKVHYGI EGAKILIENQ
IDGIKKAYDE DLIIKINTVL IPEINMNHVV DIAKELKDFV YIQNIIPLIP LYKMSHLRPP
TCEELKKVRE ECEKYIPQFR ACGQCRADAV GLIKERKILE EFFKEKNKKL NVFELKHFSH
