Reviewed, UniProtKB/Swiss-Prot Q98Q32 (DYR_MYCPU)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	folA
Ordered Locus Names:	MYPU_5370

Organism

Mycoplasma pulmonis [Complete proteome] [HAMAP]

Taxonomic identifier

2107 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.
Miscellaneous	The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 179	179	Dihydrofolate reductase		PRO_0000186397
Regions
	Domain	17 – 179	163	DHFR

Sequences

	Sequence		Length	Mass (Da)
	Q98Q32-1 [UniParc]. Last modified August 29, 2001. Version 1. Checksum: 89F35380370C9D06	FASTA	179	21,491
	10 20 30 40 50 60 MTMNLIQLLK GKWRFKMIIS IWAMTKEGLI GKDNQMPWHI KEEFQHFRRQ TLHKTLIMGK 70 80 90 100 110 120 NTFFSLPKVF DKRKMYVLSH EKDFKIDHPD VEVIYDYKDL LKEYANNDKK DIYVAGGLYV 130 140 150 160 170 YQQLIPLSDI LIVSIVKGSY EGNKYLSVDF SNFVQYKQPE IYDQFSVYYY KKKDQKNSI

References

[1]

"The complete genome sequence of the murine respiratory pathogen Mycoplasma pulmonis." Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F., Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A. Nucleic Acids Res. 29:2145-2153(2001) [PubMed: 11353084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UAB CTIP.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL445565 Genomic DNA. Translation: CAC13710.1.
PIR	A90579.
RefSeq	NP_326368.1.
3D structure databases
HSSP	HSSP built from PDB template 8DFR based on UniProtKB P00378.
ModBase	Search...
Genome annotation databases
GeneID	911218.
GenomeReviews	Gene locus MYPU_5370 in contig AL445566_GR.
KEGG	mpu:MYPU_5370.
Organism-specific databases
MypuList	MYPU_5370.
CMR	Search...
Phylogenomic databases
HOGENOM	Q98Q32.
OMA	Q98Q32. YITHILQ.
Enzyme and pathway databases
BioCyc	MPUL272635:MYPU_5370-MON.
BRENDA	1.5.1.3. 274806.
Family and domain databases
InterPro	IPR012259. DHFR. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. [Graphical view]
PANTHER	PTHR11549:SF1. DHFR. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYR_MYCPU

Accession

Primary (citable) accession number: Q98Q32

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	August 29, 2001
Last modified:	June 16, 2009
This is version 40 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)