Reviewed, UniProtKB/Swiss-Prot Q82HR6 (FOLD2_STRAW)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 2
Including the following 2 domains:
    1- Recommended name:
            Methylenetetrahydrofolate dehydrogenase
              EC=1.5.1.5
    2- Recommended name:
            Methenyltetrahydrofolate cyclohydrolase
              EC=3.5.4.9

Gene names

Name:	folD2
Ordered Locus Names:	SAV_3442

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis Methionine biosynthesis One-carbon metabolism Purine biosynthesis
Ligand	NADP
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 284	284	Bifunctional protein folD 2 HAMAP MF_01576		PRO_0000268526

Sequences

	Sequence		Length	Mass (Da)
	Q82HR6-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 9F2DCABF45B4B89D	FASTA	284	29,667
	10 20 30 40 50 60 MTAQILDGKA TAAAIKSDLT ARVAALKEKG VTPGLGTILV GDDPGSQKYV AGKHRDCAQV 70 80 90 100 110 120 GIASIQRELP ATATQEEIEA AVRELNEDPA CTGYIVQLPL PKGIDENRIL ELMDPDKDAD 130 140 150 160 170 180 GLHPMNLGRL VLNEPAPLPC TPNGVLTLLR RYGVEIKGAE VVVVGRGVTI GRPMPLLLTR 190 200 210 220 230 240 RSENATVTQC HTGTRDLSSH LKRADIIVAA AGSAHLIRPE DVKPGAAVLD VGVSRSAEGK 250 260 270 280 IVGDVHPGVA EVAGWISPNP GGVGPMTRAQ LLVNVVEAAE RSVG

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: BAC71154.1.
RefSeq	NP_824619.1.
3D structure databases
HSSP	HSSP built from PDB template 2C2X based on UniProtKB O50385.
SMR	Q82HR6. Positions 3-281.
ModBase	Search...
Genome annotation databases
GeneID	1210741.
GenomeReviews	Gene locus SAV_3442 in contig BA000030_GR.
KEGG	sma:SAV_3442.
NMPDR	fig|227882.1.peg.3445.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG328751.
OMA	KRKACAE.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV3442-MONOMER.
BRENDA	1.5.1.5. 140873. 3.5.4.9. 140873.
Family and domain databases
HAMAP	MF_01576. THF_DHG_CYH. [Tree]
InterPro	IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. IPR020630. THF_DH/CycHdrlase_cat_dom. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view]
PRINTS	PR00085. THFDHDRGNASE.
PROSITE	PS00766. THF_DHG_CYH_1. False negative. PS00767. THF_DHG_CYH_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_STRAW

Accession

Primary (citable) accession number: Q82HR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 1, 2003
Last modified:	January 19, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)