ID A0A369AUK6_9FIRM Unreviewed; 893 AA.
AC A0A369AUK6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DFR58_12022 {ECO:0000313|EMBL:RCX12723.1};
OS Anaerobacterium chartisolvens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerobacterium.
OX NCBI_TaxID=1297424 {ECO:0000313|EMBL:RCX12723.1, ECO:0000313|Proteomes:UP000253034};
RN [1] {ECO:0000313|EMBL:RCX12723.1, ECO:0000313|Proteomes:UP000253034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27016 {ECO:0000313|EMBL:RCX12723.1,
RC ECO:0000313|Proteomes:UP000253034};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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 -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|RuleBase:RU004021}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCX12723.1}.
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DR EMBL; QPJT01000020; RCX12723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369AUK6; -.
DR OrthoDB; 9800746at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000253034; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016163; F:nitrogenase activity; IEA:InterPro.
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 Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR Gene3D; 1.20.89.10; Nitrogenase Molybdenum-iron Protein, subunit B, domain 4; 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/MiaA/NifB-like_rSAM.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005980; Nase_CF_NifB.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR034165; NifB_C.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR01290; nifB; 1.
DR PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR Pfam; PF02579; Nitro_FeMo-Co; 1.
DR Pfam; PF00148; Oxidored_nitro; 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 SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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; PS00699; NITROGENASE_1_1; 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 ECO:0000256|RuleBase:RU004021};
KW Reference proteome {ECO:0000313|Proteomes:UP000253034};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 493..735
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 893 AA; 98767 MW; 5E52F603FDC1E83B CRC64;
MKNRNFTNLN INPCKVCMPM GAVMAFKGIE NSMVMLHGSQ GCSTYIRRHM AGHYNEPIDI
ASSSLNEEGT VYGGEKNLKK GLKNLIELYN PDVIGVATTC LAETIGEDIK RITSEFAESE
GLEKDRIIPM STAGYGGTGF EGYFSALLSI VKSIAKDSRP NGKINVIVGN VSPGDVRNIK
DILDSFSIDY IILPDISDTL DSPYSKEYSR IPKGGTRLED IRRMAGSSAT IELGVTIPEA
LSPGQYLLSA YNVPLYKCPI PMGIENTDLF VNILSQLSGR PVPERLVSER GRMLDGMIDS
HKYNGEGRAV IYGEPELVYA VGRLCFENGI KPVLIATGSQ NGEIKQLFKE YFSKNGMSPD
EEGKNGDFPL IIDDTDFETI QDYSVKLEAN ILIGNSDGKI ITEKEGIPLV RIGFPIHDRM
GGQRQVYTGY NGSMRLIDDI TNTLLENKYE GYRKRMYSKY YQPENQVQPA NDSRTADIDK
KTQSHPCYSS GAACSNARMH IPVAPACNIS CNYCNRKFDC VNESRPGVTS EVLTPEQAAE
KFVMVKSKLK NLKVIGIAGP GDALANFSNT KKSIELIKKL DPDITFCLST NGLMLPYYAE
ELIALGVSHV TITINTIDPT IGAKIYREIN FMGMKLYGEQ AAKLLLDNQL IGLRMLSSRG
IVCKVNIVMI KGVNDSHIPE VVKKVKECGA FMTNIMPLIP ASGSVFENME LTNNRDLTEM
RKKCEVDLKQ MYHCKQCRAD AIGILGEDVH GEFERNSCKG CAPAPAEAGR KETVYLFAVA
SKSGIMIDQH FGHAEEFYIY ESRDSKIKLL EKRNVDKYCS ESECDSEESK IEKTIKAIED
CNAVLVLRIG YRPAKALEEK GISVIQTCER IEAGIRQAVK EIEEARVVLG ARS
//