ID H0T495_9BRAD Unreviewed; 558 AA.
AC H0T495;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE {ECO:0000256|ARBA:ARBA00013280};
GN Name=nifE {ECO:0000313|EMBL:CCE01272.1};
GN ORFNames=BRAS3809_4510002 {ECO:0000313|EMBL:CCE01272.1};
OS Bradyrhizobium sp. STM 3809.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551936 {ECO:0000313|EMBL:CCE01272.1, ECO:0000313|Proteomes:UP000004098};
RN [1] {ECO:0000313|Proteomes:UP000004098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 3809 {ECO:0000313|Proteomes:UP000004098};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
CC -!- FUNCTION: This protein may play a role in the biosynthesis of the
CC prosthetic group of nitrogenase (FeMo cofactor).
CC {ECO:0000256|ARBA:ARBA00003171}.
CC -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005155}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|ARBA:ARBA00011002, ECO:0000256|RuleBase:RU004021}.
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:CCE01272.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAFJ01000392; CCE01272.1; -; Genomic_DNA.
DR RefSeq; WP_008963837.1; NZ_CAFJ01000392.1.
DR AlphaFoldDB; H0T495; -.
DR OrthoDB; 9762718at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000004098; Unassembled WGS sequence.
DR GO; GO:0016163; F:nitrogenase activity; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
DR CDD; cd01968; Nitrogenase_NifE_I; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.50.12380; Nitrogenase MoFe cofactor biosynthesis protein NifE, C-terminal; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005973; NifE.
DR NCBIfam; TIGR01283; nifE; 1.
DR PANTHER; PTHR42956; NITROGENASE IRON-MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN NIFE; 1.
DR PANTHER; PTHR42956:SF1; NITROGENASE IRON-MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN NIFE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 3: Inferred from homology;
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW ECO:0000256|RuleBase:RU004021};
KW Oxidoreductase {ECO:0000313|EMBL:CCE01272.1}.
FT DOMAIN 45..444
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
FT DOMAIN 496..544
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 558 AA; 59955 MW; E3114701A96D524E CRC64;
MSSLSATIQN VFNEPGCGKN ANKSEAERKK GCTKQLQPGG AAGGCAFDGA KVALQPLTDV
AHLVHGPIAC EGNSWDNRGA ASSGSQIWRT GFTTDINETD VVFGGEKRLY KAIKEIIEKY
DPPAVFVYQT CVPAMTGDDI NAVCKAASAK FGKPCIPVNS PGFVGPKNLG NKLAGEALLD
HVIGTVEPEV TTPYDLNIIG EYNLSGELWQ VKPLFDELGI RISACISGDG RYKEVASSHR
ARAAMMVCSK AMINVARKME ERYGIPFFEG SFYGIQDSSD SLREIARLLV ERGAPADLLD
RTEAVIAREE AKAWAAIEPF KQRLTGKKVL LITGGVKSWS VVAALQEAGM ELVGTSVKKS
TKEDKERIKE LMGQDAHMID DMAPREMYKM LKDAKADIML SGGKSQFVAL KAAMPWLDIN
QERSHAFMGY IGMVKLVAEI DKAIYNPMWE QLRKRAPWES ASNNWQAKAI AQANAEAAAL
AANPVAAEAA RRAKKICHCK SVDLGTIEDA IKAHGLTDVA GVRTHTNASG GCGACAGRVE
DILAAQRAPA APLLQAAE
//
