ID A0A2T0BL54_9CLOT Unreviewed; 894 AA.
AC A0A2T0BL54;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=nifB {ECO:0000313|EMBL:PRR84616.1};
GN ORFNames=CLVI_01390 {ECO:0000313|EMBL:PRR84616.1};
OS Clostridium vincentii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR84616.1, ECO:0000313|Proteomes:UP000239471};
RN [1] {ECO:0000313|EMBL:PRR84616.1, ECO:0000313|Proteomes:UP000239471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR84616.1,
RC ECO:0000313|Proteomes:UP000239471};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium vincentii DSM 10228.";
RL Submitted (MAR-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:PRR84616.1}.
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DR EMBL; PVXQ01000001; PRR84616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BL54; -.
DR OrthoDB; 9800746at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000239471; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000239471};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 500..742
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 894 AA; 100086 MW; 1F7ED13B7999986F CRC64;
MKDSYVNLTI NPCKMCMPMG VVSAVYGIKG AMTILHGSQG CSTYIRRHMA THYNEPIDIA
SSSLTEEGTV YGGERNLISG LENLIKLYNP EVIAIATTCL AETIGEDVAR ISKLFKETHE
DFKVKLIPIP SPGYGGTQYD GFCKALRSIV ENVEMNDSSN NKINVVCSQI SPADTRELKE
ILESFGIDYI LIPDISENLD GTHSSNYKKL PSGGTSLEEI KYMAGAKATI ELSTFVKDEY
SVGEYLQDTY NVKNYRINIP RGLRDTDKFL DVLSLVSKRP IPDKYKLQRG RYLDAMIDSH
KYNSEGRAVI FGEPDFVYST VRLALENGVM PVVIAVGEKC PSLEALLKEE VSELGKQLFV
DNFKIMDEAD FKDIENYAVE FKANVMIGSS DGRRIEEKRG IPLVRVSFPI HDRVGGQRIL
SIGYEGSLNL GDKIANVVLQ TKESTFRETL YRELYKGEKK MDLKKIEAKT VEISIEKPKH
VEISIEEKTK THPCFSCDSA HKYARMHLPI APKCNVSCNY CLRKFDCVNE SRPGVTTDVL
SPEEAFEKYK YVKGKMDNLK VVGIAGPGDA LANFDEVRKT LKLIKEYDND VTFCLSTNGL
MLPFYAQELI DLGVSHVTVT MNAIDPKITA KVYKYIDYLG VTYTGEEGTQ ILLNNQLSGI
KYLADRGIMV KVNIVMLKGI NDHHIEAVTK KVKELGAGIT NIMQMIPVKG SVFQDMPLTS
NKEIMSLRKK CEENIKQMYH CKQCRADAIG LLGDDQSAKY SNEAIKEEKN NTQLKFAVAT
KSGMVVDQHF GHVSEFYIYE YKDGVAMFLE KRDIEKYCNG KDVCEEEEDK FNRISKTVED
CTGVICLRIG GEPSKKLKEL GVGIFMTCER VEVAVVAAAE EILSGIKNKR ILTV
//
