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Q89B13 (METF_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5,10-methylenetetrahydrofolate reductase

EC=1.5.1.20
Gene names
Name:metF
Ordered Locus Names:bbp_047
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.

Cofactor

FAD By similarity.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion.

Sequence similarities

Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytosol

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmethylenetetrahydrofolate reductase (NAD(P)H) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2952955,10-methylenetetrahydrofolate reductase
PRO_0000190260

Regions

Nucleotide binding28 – 336NAD By similarity
Nucleotide binding59 – 624FAD By similarity
Nucleotide binding59 – 602NAD By similarity
Nucleotide binding119 – 1213FAD By similarity
Nucleotide binding132 – 1332FAD By similarity
Nucleotide binding157 – 1604FAD By similarity
Nucleotide binding166 – 1738FAD By similarity

Sites

Active site281Proton donor/acceptor By similarity
Binding site891FAD By similarity
Binding site1211Substrate By similarity
Binding site1531FAD By similarity
Binding site1841Substrate By similarity
Binding site2201Substrate By similarity
Binding site2241Substrate By similarity
Binding site2761Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89B13 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D34F60F04D44AED3

FASTA29533,770
        10         20         30         40         50         60 
MKLVYKNYHE TLNQHLMNIC EKVNISFEFF PPNNILSEKN LWQVIDKLKL LTPKFFSVTH 

        70         80         90        100        110        120 
GTNSKIRATC TSNIVKKIKK YTGIETVPHL TCINSTEEEL KVIAKTYWDS GIRHILALRG 

       130        140        150        160        170        180 
DIFNTNCKPK IYAVDLIKLL KSIANFEISV AAYPEVHPEA VNAKYDIINL KRKVEAGATR 

       190        200        210        220        230        240 
AITQFFFNID CFLRFRDLCV KNNITIDIVP GIFPISNFKQ LLKFSSVSNV SIPKWLCCMF 

       250        260        270        280        290 
HGLDNDLNTS RIIGSSIAID MVKVLYSEGI RSFHFYTLNK SEISFAICKI LENKS 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26786.1.
RefSeqNP_777681.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89B13.
SMRQ89B13. Positions 22-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp047.

Proteomic databases

PRIDEQ89B13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26786; AAO26786; bbp_047.
GeneID1058532.
KEGGbab:bbp047.
PATRIC21244867. VBIBucAph80364_0044.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0685.
KOK00297.
OMAFIRAETG.
OrthoDBEOG6D2KVW.
ProtClustDBPRK09432.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-47-MONOMER.
UniPathwayUPA00193.

Family and domain databases

InterProIPR003171. Mehydrof_redctse.
IPR004620. MTHF_reductase_bac.
[Graphical view]
PfamPF02219. MTHFR. 1 hit.
[Graphical view]
TIGRFAMsTIGR00676. fadh2. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMETF_BUCBP
AccessionPrimary (citable) accession number: Q89B13
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: June 1, 2003
Last modified: December 11, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways