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Q82QG3 (FOLD1_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein FolD 1

Including the following 2 domains:

  1. Methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.5
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
Gene names
Name:folD1
Ordered Locus Names:SAV_543
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate By similarity. HAMAP MF_01576

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP MF_01576

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP MF_01576

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_01576

Subunit structure

Homodimer By similarity. HAMAP MF_01576

Sequence similarities

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287Bifunctional protein FolD 1 HAMAP MF_01576
PRO_0000268525

Sequences

Sequence LengthMass (Da)Tools
Q82QG3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8B7F00B17DBB5C1C

FASTA28729,760
        10         20         30         40         50         60 
MSATQTAQLM DGTGHARRIV EEAAAKAAEI SQRTGTAPCL ATVLVGDDPA SVTYVRMKRA 

        70         80         90        100        110        120 
RCAKAGIRSR HIALPATTTT AELIDSLSGL SGDPEVHGIL LQHPCGPHID ERAAFEAIAP 

       130        140        150        160        170        180 
AKDVDGVTMH SFAAMSFGLP GFVSCTPGGI MRLLEAYDVD LAGKHAVVVG RSAILGKPVG 

       190        200        210        220        230        240 
MLLLAKDATV TYCHSRTADL SAMVREADVV VAAVGRPRLI RGEDIKPGAV VIDAGYNPGN 

       250        260        270        280 
VGDVDFDAVL TRARLITPVP GGVGPMTIAV LLEQTVDAAA NQLGVQQ

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000030 Genomic DNA. Translation: BAC68253.1.
RefSeqNP_821718.1. NC_003155.4.

3D structure databases

HSSPHSSP built from PDB template 1A4I based on UniProtKB P11586.
ProteinModelPortalQ82QG3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1210049.
GenomeReviewsGene locus SAV_543 in contig BA000030_GR.
KEGGsma:SAV_543.
NMPDRfig|227882.1.peg.544.
PATRIC23714356. VBIStrAve112782_0596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG328751.
OMAGPMTINT.
ProtClustDBCLSK915313.

Enzyme and pathway databases

BioCycSAVE227882:SAV543-MONOMER.

Family and domain databases

HAMAPMF_01576. THF_DHG_CYH.
[Tree]
InterProIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK01491.
PfamPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
PROSITEPS00766. THF_DHG_CYH_1. False negative.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFOLD1_STRAW
AccessionPrimary (citable) accession number: Q82QG3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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