Reviewed, UniProtKB/Swiss-Prot Q82QG3 (FOLD1_STRAW)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 1
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:	folD1
Ordered Locus Names:	SAV_543

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 pathway. HAMAP MF_01576
Subunit structure	Homodimer By similarity.
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 compound 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 – 287	287	Bifunctional protein folD 1 HAMAP MF_01576		PRO_0000268525

Sequences

	Sequence		Length	Mass (Da)
	Q82QG3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 8B7F00B17DBB5C1C	FASTA	287	29,760
	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

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
EMBLGenBankDDBJ	BA000030 Genomic DNA. Translation: BAC68253.1.
RefSeq	NP_821718.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBase	Search...
Genome annotation databases
GeneID	1210049.
GenomeReviews	Gene locus SAV_543 in contig BA000030_GR.
NMPDR	fig|227882.1.peg.544.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q82QG3.
OMA	Q82QG3. GFGRMAM.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV543-MON.
BRENDA	1.5.1.5. 140873. 3.5.4.9. 140873.
Family and domain databases
HAMAP	MF_01576. [Tree]
InterPro	IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. [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.
ProDom	PD002300. THFDhg/Cyc_hydro. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00766. THF_DHG_CYH_1. False negative. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD1_STRAW

Accession

Primary (citable) accession number: Q82QG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 37 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)