ID A0A094JDE5_9GAMM Unreviewed; 450 AA.
AC A0A094JDE5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HR45_08680 {ECO:0000313|EMBL:KFZ37905.1};
OS Shewanella mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ37905.1, ECO:0000313|Proteomes:UP000029264};
RN [1] {ECO:0000313|EMBL:KFZ37905.1, ECO:0000313|Proteomes:UP000029264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YQH10 {ECO:0000313|EMBL:KFZ37905.1,
RC ECO:0000313|Proteomes:UP000029264};
RA Liu Y., Zeng R.;
RT "Shewanella sp. YQH10.";
RL Submitted (JUN-2014) 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:KFZ37905.1}.
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DR EMBL; JPEO01000004; KFZ37905.1; -; Genomic_DNA.
DR RefSeq; WP_037441997.1; NZ_JPEO01000004.1.
DR AlphaFoldDB; A0A094JDE5; -.
DR STRING; 1515746.HR45_08680; -.
DR eggNOG; COG0535; Bacteria.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000029264; 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:UP000029264};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 48..297
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 48622 MW; F383AA6E365B7D91 CRC64;
MELHTDERLS AASTGCSSSQ AEGASVSHLL PKDVQQQIAR HPCYSKQAHK YARMHLPVAP
ACNIQCNYCN RKYDCSNESR PGVVSHLVDP HGALKQFRAI KKRAPNLTVV GIAGPGDALA
NPKATFSALK LIREEDPTAQ LCISTNGLML AEYADELAAH GVHHLTITIN TIDPVIAAKI
YPWVYYNHRR LRGLAAAERL IANQLAGLEA AAKLGMLVKV NTVLIPGIND QQIATLSAAV
KARGALMHNI MPLISAAEHG TYFGVTGQRG PTEAELSSAR DASGQFMPQM THCQQCRADA
VGTLGGGCGT EAASETSQPI KIAVATNGGP LINTHFGHAQ QFEIYQLDSA TTEFHFLERR
QVAQYCNGAS ECPEEEADKQ AMFKAIEDCR MVLCSRIGIA PWRTLEQMGI TPNVDHAFAP
IDEALATLAK TQLAPKADSH KESNDEVCHY
//
