NIFB_KLEPN
ID NIFB_KLEPN Reviewed; 468 AA.
AC P10390;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL J. Mol. Biol. 203:715-738(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029020; DOI=10.1128/jb.169.3.1120-1126.1987;
RA Buikema W.J., Klingensmith J.A., Gibbons S.L., Ausubel F.M.;
RT "Conservation of structure and location of Rhizobium meliloti and
RT Klebsiella pneumoniae nifB genes.";
RL J. Bacteriol. 169:1120-1126(1987).
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; X13303; CAA31683.1; -; Genomic_DNA.
DR EMBL; M15545; AAA25107.1; -; Genomic_DNA.
DR PIR; S02514; S02514.
DR AlphaFoldDB; P10390; -.
DR SMR; P10390; -.
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; IPR006638; Elp3/MiaB/NifB.
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 SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 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 S-adenosyl-L-methionine.
FT CHAIN 1..468
FT /note="FeMo cofactor biosynthesis protein NifB"
FT /id="PRO_0000153041"
FT DOMAIN 40..289
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 54
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 58
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 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 61
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 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT BINDING 288
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT CONFLICT 141
FT /note="V -> M (in Ref. 2; AAA25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> G (in Ref. 2; AAA25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> D (in Ref. 2; AAA25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="G -> R (in Ref. 2; AAA25107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 50856 MW; 89BF828E3E73FE1E CRC64;
MTSCSSFSGG KACRPADDSA LTPLVADKAA AHPCYSRHGH HRFARMHLPV APACNLQCNY
CNRKFDCSNE SRPGVSSTLL TPEQAVVKVR QVAQAIPQLS VVGIAGPGDP LANIARTFRT
LELIREQLPD LKLCLSTNGL VLPDAVDRLL DVGVDHVTVT INTLDAEIAA QIYAWLWLDG
ERYSGREAGE ILIARQLEGV RRLTAKGVLV KINSVLIPGI NDSGMAGVSR ALRASGAFIH
NIMPLIARPE HGTVFGLNGQ PEPDAETLAA TRSRCGEVMP QMTHCHQCRA DAIGMLGEDR
SQQFTQLPAP ESLPAWLPIL HQRAQLHASI ATRGESEADD ACLVAVASSR GDVIDCHFGH
ADRFYIYSLS AAGMVLVNER FTPKYCQGRD DCEPQDNAAR FAAILELLAD VKAVFCVRIG
HTPWQQLEQE GIEPCVDGAW RPVSEVLPAW WQQRRGSWPA ALPHKGVA
