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Q8KA62 (METF_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_043
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length292 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 – 2922925,10-methylenetetrahydrofolate reductase
PRO_0000190259

Regions

Nucleotide binding28 – 336NAD By similarity
Nucleotide binding59 – 624FAD By similarity
Nucleotide binding59 – 602NAD By similarity
Nucleotide binding118 – 1203FAD By similarity
Nucleotide binding131 – 1322FAD By similarity
Nucleotide binding156 – 1594FAD By similarity
Nucleotide binding165 – 1728FAD By similarity

Sites

Active site281Proton donor/acceptor By similarity
Binding site881FAD By similarity
Binding site1201Substrate By similarity
Binding site1521FAD By similarity
Binding site1831Substrate By similarity
Binding site2191Substrate By similarity
Binding site2231Substrate By similarity
Binding site2751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KA62 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0660895E1B065E71

FASTA29233,676
        10         20         30         40         50         60 
MNFLHQYYQD IIKKKLENLN DKIQCSFEFF PPKNLDTEKK LFSSVVKLSL LKPFLFSVTY 

        70         80         90        100        110        120 
GANSGERKKT YSIVQRIHKK TGITTAPHLT CVDASLSELK EIAKFYWENG IRSIVALRGD 

       130        140        150        160        170        180 
VPNKSYQHKI YALDLVVLLK KIADFDISVA AYPEIHPESK NAQSDILNLK KKADAGANRA 

       190        200        210        220        230        240 
ITQFFFNVES YLRFRDNCIK NNINIEIIPG ILPIYNFEQL KKFSSMTNVS IPKWMFEMFN 

       250        260        270        280        290 
GLDEDLETQK IIGSNIVINI VKTLLYEGVK NFHFYTLNKS DVIYSICHMF GL 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67614.1.
RefSeqNP_660403.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8KA62.
SMRQ8KA62. Positions 22-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67614; AAM67614; BUsg_043.
GeneID1005859.
KEGGbas:BUsg043.
PATRIC21246851. VBIBucAph100086_0043.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0685.
KOK00297.
OMAFIRAETG.
OrthoDBEOG6D2KVW.
ProtClustDBPRK09432.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-48-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_BUCAP
AccessionPrimary (citable) accession number: Q8KA62
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: December 11, 2013
This is version 71 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names