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Database: UniProt
Entry: A0A218Q716_9CYAN
LinkDB: A0A218Q716_9CYAN
Original site: A0A218Q716_9CYAN 
ID   A0A218Q716_9CYAN        Unreviewed;       480 AA.
AC   A0A218Q716;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=NIES3585_37250 {ECO:0000313|EMBL:GAX37680.1};
OS   Nodularia sp. NIES-3585.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Nodularia.
OX   NCBI_TaxID=1973477 {ECO:0000313|EMBL:GAX37680.1, ECO:0000313|Proteomes:UP000198352};
RN   [1] {ECO:0000313|EMBL:GAX37680.1, ECO:0000313|Proteomes:UP000198352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3585 {ECO:0000313|EMBL:GAX37680.1,
RC   ECO:0000313|Proteomes:UP000198352};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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}.
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:GAX37680.1}.
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DR   EMBL; BDUB01000001; GAX37680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218Q716; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000198352; Unassembled WGS sequence.
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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR   SMART; SM00729; Elp3; 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          55..306
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  53253 MW;  3DABCC29F2E4AF7B CRC64;
     MILPSNGLLT SSNQEPASTQ AKSGGCGCDS STTVEMDQKL QERIAQHPCY SEDAHHHYAR
     MHVAVAPACN IQCNYCNRKY DCANESRPGV VSELLTPEEA AHKALVIAGK IPQMTVVGIA
     GPGDPLANPE KTFRTFELIA DKAPDIKLCL STNGLMLTEY IDRIKQLNID HVTITLNTID
     PEIGAQIYSW VHYKRKRYRG VEGAKILLEK QMEGLQALRE ADILCKVNSV MIPGINDQHL
     IEVNKMIREN GAFLHNIMPL ISAPEHGTHF GLTGQRGPTP KEVKSVQDNC AGNMKMMRHC
     RQCRADAVGL LGEDRSQEFT KDKFLEMTPE YDLEQRTLVH EGIEKFKEEL KIAKDKASAG
     KKFANNPKIL VAVATKGGGL VNQHFGHAKE FQIYEVDGNQ VTFVSHRKID QYCQGGFSEE
     ATFEHIMAAI ADCKAVLVSK IGNCPQEKLQ AAGIQTVEAY DVIEKVALEF YEQYVKELGN
//
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