ID   NIFB_CHLTE              Reviewed;         424 AA.
AC   Q8KC85;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=FeMo cofactor biosynthesis protein NifB {ECO:0000305|PubMed:29250084};
DE            EC=4.-.-.- {ECO:0000305|PubMed:29250084};
DE   AltName: Full=FeMo-cofactor maturase NifB {ECO:0000303|PubMed:29250084};
DE   AltName: Full=Nitrogenase cofactor maturase NifB;
DE   AltName: Full=Radical SAM assemblase NifB;
GN   Name=nifB {ECO:0000303|PubMed:29250084};
GN   OrderedLocusNames=CT1540 {ECO:0000312|EMBL:AAM72766.1};
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN   [2]
RP   FUNCTION, COFACTOR, SUBUNIT, AND PATHWAY.
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=29250084; DOI=10.3389/fpls.2017.01947;
RA   Arragain S., Jimenez-Vicente E., Scandurra A.A., Buren S., Rubio L.M.,
RA   Echavarri-Erasun C.;
RT   "Diversity and Functional Analysis of the FeMo-Cofactor Maturase NifB.";
RL   Front. Plant Sci. 8:1947-1947(2017).
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. {ECO:0000269|PubMed:29250084}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:29250084};
CC       Note=Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two
CC       others probably act as substrate. {ECO:0000250|UniProtKB:D5VRM1};
CC   -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC       {ECO:0000305|PubMed:29250084}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29250084}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. NifB family.
CC       {ECO:0000305}.
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DR   EMBL; AE006470; AAM72766.1; -; Genomic_DNA.
DR   RefSeq; NP_662424.1; NC_002932.3.
DR   RefSeq; WP_010933205.1; NC_002932.3.
DR   AlphaFoldDB; Q8KC85; -.
DR   SMR; Q8KC85; -.
DR   STRING; 194439.CT1540; -.
DR   EnsemblBacteria; AAM72766; AAM72766; CT1540.
DR   KEGG; cte:CT1540; -.
DR   PATRIC; fig|194439.7.peg.1393; -.
DR   eggNOG; COG0535; Bacteria.
DR   eggNOG; COG1433; Bacteria.
DR   HOGENOM; CLU_027639_0_0_10; -.
DR   OMA; NHPCYSE; -.
DR   OrthoDB; 1199289at2; -.
DR   UniPathway; UPA00782; -.
DR   Proteomes; UP000001007; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.420.130; -; 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/MiaB/NifB.
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   PANTHER; PTHR43787:SF3; PTHR43787:SF3; 1.
DR   Pfam; PF02579; Nitro_FeMo-Co; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF53146; SSF53146; 1.
DR   TIGRFAMs; TIGR01290; nifB; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Nitrogen fixation;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..424
FT                   /note="FeMo cofactor biosynthesis protein NifB"
FT                   /id="PRO_0000447344"
FT   DOMAIN          12..261
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         30
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P69848"
FT   BINDING         257
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT   BINDING         260
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:D5VRM1"
SQ   SEQUENCE   424 AA;  46794 MW;  1FBBE838B7F43F78 CRC64;
     MTLNIKNHPC FNDSSRHTYG RIHLPVAPKC NIQCNYCNRK FDCMNENRPG ITSKVLSPRQ
     ALYYLDNALK LSPNISVVGI AGPGDPFANP EETMETLRLV REKYPEMLLC VATNGLDMLP
     YIEELAELQV SHVTLTINAI DPEIGQEIYA WVRYQKKMYR DRQAAELLLE NQLAALQKLK
     RYGVTAKVNS IIIPGVNDQH VIEVARQVAS MGADILNALP YYNTTETVFE NIPEPDPMMV
     RKIQEEAGKL LPQMKHCARC RADAVGIIGE INSDEMMAKL AEAALMPKNP DEHRPYIAVA
     SLEGVLINQH LGEADRFLVY ALDEEKKSCT LVDSRQAPPP GGGKLRWEAL AAKLSDCRAV
     LVNSAGDSPQ SVLKASGIDV MSIEGVIEEA VYGVFTGQNL KHLMKSSQIH ACKTSCGGDG
     NGCD