ID Q6J2L8_CLOPA Unreviewed; 929 AA.
AC Q6J2L8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 91.
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 Name=nifN-B {ECO:0000313|EMBL:AAT37646.1};
OS Clostridium pasteurianum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501 {ECO:0000313|EMBL:AAT37646.1};
RN [1] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RX PubMed=3457003;
RA Chen K.C.K., Chen J.-S., Johnson J.L.;
RT "Structural features of multiple nifH-like sequences and very biased codon
RT usage in nitrogenase genes of Clostridium pasteurianum.";
RL J. Bacteriol. 166:162-172(1986).
RN [2] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RX PubMed=3473447; DOI=10.1093/nar/15.9.3935;
RA Wang S.-Z., Chen J.-S., Johnson J.L.;
RT "Nucleotide and deduced amino acid sequences of nifD encoding the alpha-
RT subunit of nitrogenase MoFe protein of Clostridium pasteurianum.";
RL Nucleic Acids Res. 15:3935-3935(1987).
RN [3] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RX PubMed=2840948; DOI=10.1021/bi00408a021;
RA Wang S.-Z., Chen J.-S., Johnson J.L.;
RT "Distinct structural features of the alpha and beta subunits of nitrogenase
RT molybdenum-iron protein of Clostridium pasteurianum: an analysis of amino
RT acid sequences.";
RL Biochemistry 27:2800-2810(1988).
RN [4] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RX PubMed=2726466; DOI=10.1093/nar/17.8.3299;
RA Wang S.-Z., Chen J.-S., Johnson J.L.;
RT "Nucleotide and deduced amino acid sequences of nifE from Clostridium
RT pasteurianum.";
RL Nucleic Acids Res. 17:3299-3299(1989).
RN [5] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RX PubMed=2022611;
RA Wang S.-Z., Dean D.R., Chen J.-S., Johnson J.L.;
RT "The N-terminal and C-terminal portions of NifV are encoded by two
RT different genes in Clostridium pasteurianum.";
RL J. Bacteriol. 173:3041-3046(1991).
RN [6] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RA Wang S.Z., Chen K.C., Toth J., Johnson J.L., Chen J.S.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AAT37646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AAT37646.1};
RA Chen J.S.;
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|RuleBase:RU004021}.
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DR EMBL; AY603957; AAT37646.1; -; Genomic_DNA.
DR RefSeq; WP_003447864.1; NZ_LFYL01000003.1.
DR AlphaFoldDB; Q6J2L8; -.
DR GeneID; 76625867; -.
DR OrthoDB; 9800746at2; -.
DR UniPathway; UPA00782; -.
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; cd03466; Nitrogenase_NifN_2; 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; SFLDS00029; Radical_SAM; 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 504..753
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 929 AA; 103097 MW; 5C545ED9BFAA2E2F CRC64;
MNSRNFVNLN VNPCKMCMPM GGVMAFKGIE GNMVILHGSQ GCSTYIRRHM ATHYNEPIDI
ASSSLTENGT VYGGTKNLKL GLKNMIEMYN PKTIGIMTTC LAETIGEDIQ RILHEFREEE
KGNEVYENIK IMTTSTPGYG GTQAEGYFRA LRSIVEQICK KPENDVKLNK INIICANLNP
GDVRNIKEIL ETFGVEYTIL PDVSNTLDSS HNDQYTRLPA GGTKIEDIEK MGSALATIEM
GMTVPYDYSP GTYLKEEFGV PLYKCNIPMG LRSTDEFMSI ISKITGKSMP DKIKLQRGRY
LDAMIDSHKY NAEARAVIYG EPELVLAITK TCAENGVLVK LIATGSKNKE LKAKLEKELA
RQVEKPVILD DTDFETIESY AKDFNINVMI GNSDGRRMAG RLGVKIVRIG FPVHDRIGAQ
RLIFTGYNGS AFFIDSIANT ILEDKEDTFR KDSYDRFFIP KKEGEDNMEI ANKTNVTIEE
PLVEEKVLSK KELNAKKSCT HPCYGDNAHK FARMHIPVAP SCNISCNYCN RKYDCTNESR
PGVTSQVLSP EGALAKFKAV KAKFKNLTVL GIAGPGDALA NFDVVKKSIE LIKKEDPNIT
FCISTNGLML PFFANQLIEL GVSHVTVTMN SVDKKIGAKI YREVNYIGKK YTGEEAADIL
MHNQLSGLKY LSSKGVVCKV NIVMIKGVND THIPEVVKKA KECGAFMTNI MKLIPVEGTA
FENMPETTTK ELNDMRKACE IDMKQMYHCK QCRADAIGTL GNDCSADFSD IAPAGDCKSG
CSSSIVDAYQ DKVEVPEENS TRMSKYRFAI ASKSGVDIDQ HFGQAKEFQI YAYEGGDIKF
LESRDVDQYC TGTDDCGEHE NKIMKIVKTI HDCDAVLALR AGIEPVKTLE SEGIKLIQMY
DSINRGIKRA VEEMAAQGGE EVKDGKITI
//