GenomeNet

Database: UniProt
Entry: A0A369AUK6_9FIRM
LinkDB: A0A369AUK6_9FIRM
Original site: A0A369AUK6_9FIRM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system