ID H2J2H8_RAHAC Unreviewed; 464 AA.
AC H2J2H8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 OrderedLocusNames=Rahaq2_5094 {ECO:0000313|EMBL:AEX54795.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OG Plasmid pRahaq202 {ECO:0000313|EMBL:AEX54795.1,
OG ECO:0000313|Proteomes:UP000009010}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX54795.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX54795.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RC PLASMID=pRahaq202 {ECO:0000313|EMBL:AEX54795.1};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RC PLASMID=pRahaq202 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of plasmid 2 of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) 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}.
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DR EMBL; CP003246; AEX54795.1; -; Genomic_DNA.
DR RefSeq; WP_014333904.1; NZ_JMPO01000160.1.
DR AlphaFoldDB; H2J2H8; -.
DR GeneID; 61514969; -.
DR KEGG; raq:Rahaq2_5094; -.
DR PATRIC; fig|745277.3.peg.4862; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_027639_0_0_6; -.
DR OrthoDB; 9785734at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000009010; Plasmid pRahaq202.
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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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; SFLDG01068; FeMo_cofactor_biosynthesis_pro; 1.
DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR SMART; SM00729; Elp3; 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 Plasmid {ECO:0000313|EMBL:AEX54795.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 37..275
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 464 AA; 50269 MW; 1E13FEABD606D896 CRC64;
MTSCPSSAGC SGQSPSRVNE QLARKAAQHP CYSVSGHHRF ARMHLAVAPA CNLQCHYCNR
KYDCSNESRP GVVSELLLPE QAVAKARQVA AAIPQLSVVG IAGPGDPLAN IGRTFQTLEL
LRQQLPDLKL CLSTNGLMLP DVVDRLVDIG VDHVTVTMNA LDPAVAEKIY AWLWYEGERY
TGRMAADLLI ERQAEGIRKL IEKGVLVKIN SVLIPGINDQ HMQAVSQQAG EWGAFLHNIM
PLISRPEHGT VFGLNGQAEP DADMVASVRK SCGMSMPQMT HCHQCRADAI GMLGEDRNAA
FPLASVPVNP PPYLPVLHQR AQLHASIVSQ GGSEEADACL VAVATSQGQA VDQHFGHADR
FTLYSLSAAG VMQVGQRFTP RYCRSPDDCE PEDAAQNMDA LLELLADVKA VFCARIGLTP
WKRLEAAGIE PQVDGAWQPV ETALAQWWQQ RKLAGGEISI RGVA
//
