ID A0A4R3N221_9GAMM Unreviewed; 502 AA.
AC A0A4R3N221;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, 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 ORFNames=EDC35_102246 {ECO:0000313|EMBL:TCT22915.1};
OS Thiobaca trueperi.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Chromatiales; Chromatiaceae; Thiobaca.
OX NCBI_TaxID=127458 {ECO:0000313|EMBL:TCT22915.1, ECO:0000313|Proteomes:UP000295717};
RN [1] {ECO:0000313|EMBL:TCT22915.1, ECO:0000313|Proteomes:UP000295717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13587 {ECO:0000313|EMBL:TCT22915.1,
RC ECO:0000313|Proteomes:UP000295717};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TCT22915.1}.
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DR EMBL; SMAO01000002; TCT22915.1; -; Genomic_DNA.
DR RefSeq; WP_132976039.1; NZ_SMAO01000002.1.
DR AlphaFoldDB; A0A4R3N221; -.
DR OrthoDB; 9785734at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000295717; Unassembled WGS sequence.
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 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 InterPro; IPR058240; rSAM_sf.
DR NCBIfam; TIGR01290; nifB; 1.
DR PANTHER; PTHR43787:SF13; 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; SFLDG01068; 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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:UP000295717};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 50..299
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 502 AA; 54459 MW; 8B0816346839A23A CRC64;
MALTIVSQSG GAAGGCASSG CGSSTDRLAH LPEAIRAKVN NHPCFSEDAH HHYARMHVAV
APACNIQCHY CNRKYDCSNE SRPGVVSEVL TPDQAVKKVM AVAATIPQMT VLGIAGPGDP
LANPERTLET FRQLSAKAPD IKLCVSTNGL ALPAVVDELC QHNIEHVTIT INCVDPDVGA
KIYPWIFWNN RRIKGRKAAE ILIEQQQKGL EMLVARGVLV KVNSVLIPGV NDEHLKEVSR
VVKAKGAFLH NVMPLIAEAE HGTFYGIMGQ RGPTTDELQR LQDACAGDMA MMRHCRQCRA
DAVGMLGEDR GHEFTLDRIE HLEIDYAAAM ARRAEVHAAI EANRAAQRRQ SGEAFVSLAS
LTRRLPAKPE SRPVLMAVAS TGGGVVNQHF GHAREFLIYE ATAQDVRFIG ARKVDLYCTG
DETCGEAETS LQKTIRTLAG CEVVLCARIG YEPWGQLEAA GILPNGEHAL EPIEEAVTAV
YREMQESGRL DQSAPAQQRL SA
//
