ID Q47G28_DECAR Unreviewed; 500 AA.
AC Q47G28;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=Daro_1454 {ECO:0000313|EMBL:AAZ46203.1};
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ46203.1};
RN [1] {ECO:0000313|EMBL:AAZ46203.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCB {ECO:0000313|EMBL:AAZ46203.1};
RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT "Complete sequence of Dechloromonas aromatica RCB.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000089; AAZ46203.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47G28; -.
DR STRING; 159087.Daro_1454; -.
DR KEGG; dar:Daro_1454; -.
DR eggNOG; COG0535; Bacteria.
DR eggNOG; COG1433; Bacteria.
DR HOGENOM; CLU_027639_0_0_4; -.
DR OrthoDB; 9785734at2; -.
DR UniPathway; UPA00782; -.
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; SFLDG01068; FeMo_cofactor_biosynthesis_pro; 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 52..301
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 500 AA; 54385 MW; B729A4C971CF740B CRC64;
MELPVISNTA PAAEGGGCSS SGCGTAPDAL GHLPDHIRAK VQDHPCYSEE AHHYFARMHV
AVAPACNIQC NYCNRKYDCS NESRPGVVSE LLTPDQAIKK VLAVAAEIPQ MTVLGIAGPG
DPLANPGRTF ETFEQLSARA PDIKLCVSTN GLNLPQYVDR IAQHNIDHVT ITINCVDPEV
GAKIYPWIYW ENKRITGVEG ARILIEQQQK GLQMLTDRGI LVKVNSVLIP GVNDEHLKEV
SKIVKAKGAF LHNVMPLIAE PEHGTYYGIM EQPEPTPEML QDLQDACAGD MAMMRHCRQC
RADAVGLLGE DRGDEFTLDK IDVMDVDYEA AMVRRKVVHD EIIEKLDAKR GIVKPKHEGI
PEGSRPVLMA VAGKNGVVAE HFGHAKEFLI YEASPSGVRF ISHRKTELYC GGMDSCGNGD
VVDEGATESL LDRNIRVLEG CEVVLCSKIG YEPWGKLEAA GIAPNGEHAM EPIEDAVMAV
YKEIAATGKL LPSAETLKVA
//
