ID Q5NLG9_ZYMMO Unreviewed; 489 AA.
AC Q5NLG9;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
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=ZMO1817 {ECO:0000313|EMBL:AAV90441.1};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV90441.1, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV90441.1, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV90441.1; -; Genomic_DNA.
DR RefSeq; WP_011241550.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NLG9; -.
DR STRING; 264203.ZMO1817; -.
DR KEGG; zmo:ZMO1817; -.
DR eggNOG; COG0535; Bacteria.
DR eggNOG; COG1433; Bacteria.
DR HOGENOM; CLU_027639_0_0_5; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000001173; Chromosome.
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:UP000001173};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 59..310
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 54718 MW; 1A7AB44982002E7B CRC64;
MSQLIHIQPL EPNGGIPSPR PATQGCASSA CGKMSDAKDL ADDIWEKVKD HPCYSEEAHQ
YFARMHVAVA PACNIQCNYC NRKYDCANES RPGVVSERLT PEQALRKVIA VANEVSQLSV
LGIAGPGDAC YDWEKTKETF EQVAKVIPDV KFCLSTNGLA LADCIDDIAK MNIDHVTLTI
NMVDPEIGAK IYPWIFFENK RWTGIEASRI LHERQMLALE LLKERGILTK VNSVMIPNIN
DTHLLEVNRV VKEKGAFLYN IMPLISDPAH GTHFGLTRQR EPSHQELMAL QNQLADGTKL
MRHCRQCRAD AIGLLGEDRG QAFSMDKIPE TLEYNPANRA SYREIVAQER GEHLEQKKSA
EKKLAELEAK PTILAAVVSK QGGRINQHFG HAQEFQIYEV SPYGVKFISH RKIPLYCAEG
NGDDQRLDSI ITALEGIQAV LCARIGDCPR EKLEKAGIEV NVDYAHDWIE SGLSSWYAAR
FSKENRRIA
//
