ID T0Z5B2_9BACT Unreviewed; 521 AA.
AC T0Z5B2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:EQD24960.1};
GN ORFNames=D084_Lepto4C00301G0005 {ECO:0000313|EMBL:EQD24960.1};
OS Leptospirillum sp. Group IV 'UBA BS'.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1260983 {ECO:0000313|EMBL:EQD24960.1, ECO:0000313|Proteomes:UP000017751};
RN [1] {ECO:0000313|EMBL:EQD24960.1, ECO:0000313|Proteomes:UP000017751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23645189; DOI=10.1128/AEM.00202-13;
RA Goltsman D.S., Dasari M., Thomas B.C., Shah M.B., VerBerkmoes N.C.,
RA Hettich R.L., Banfield J.F.;
RT "New group in the Leptospirillum clade: cultivation-independent community
RT genomics, proteomics, and transcriptomics of the new species
RT "Leptospirillum group IV UBA BS".";
RL Appl. Environ. Microbiol. 79:5384-5393(2013).
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:EQD24960.1}.
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DR EMBL; AURA01000301; EQD24960.1; -; Genomic_DNA.
DR AlphaFoldDB; T0Z5B2; -.
DR PATRIC; fig|1260983.3.peg.731; -.
DR HOGENOM; CLU_027639_0_0_0; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000017751; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000017751};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 56..305
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 521 AA; 57167 MW; 2662441B42A11597 CRC64;
MDSRDTDFLK IIQEPETEAS GCSEKATCGS SAGPADMDPE VWNKVKNHPC YSEEAHHFYA
RMHVAVAPAC NIQCNYCNRK YDCSNESRPG VVSERLTPEL AAKKVLAVAS EIHQMTVVGI
AGAGDSLANP DKTFKTFELI SKAAPDIKLC LSTNGLALPD MVDRIADYNV DHVTVTINMV
DPEVGEKIYP WIFYNKKRWK GRDAAKILSE RQLLGLEMLT ARKILVKVNS VMIPGINDSH
LKDVNREVKK RGAFLHNIMP LISEPEHGTF YGLTGQRGPT AEELKALQDS CEGEMNMMRH
CRQCRADAVG LLGEDRSAEF TNEKIEAIEI ADVSYDLSAR EAYRDKVEGI REKERKIKEM
LVAGLGRDSG IGQAPPILVA VATQGGGEIN QHFGHAREFQ VYEVSAADAK FVGHRRVDLY
CEGGYGEEDS LGRITAALSD CVAVMVAKIG GCPKKTLEEA RIFGIDKYAY QSIKPSLLSY
FAEYVEGVKA GRITPKASGS QTPIRSGAFT PTGQIPLTVL S
//
