dfrA

Functionⁱ

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).By similarity

Catalytic activityⁱ

5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.PROSITE-ProRule annotation

Pathwayⁱ: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:

Dihydrofolate reductase (dfrA)

This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	27	SubstrateBy similarity	1
Binding siteⁱ	57	SubstrateBy similarity	1
Binding siteⁱ	114	SubstrateBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	6 – 7	NADPBy similarity	2
Nucleotide bindingⁱ	14 – 19	NADPBy similarity	6
Nucleotide bindingⁱ	43 – 46	NADPBy similarity	4
Nucleotide bindingⁱ	62 – 65	NADPBy similarity	4
Nucleotide bindingⁱ	95 – 100	NADPBy similarity	6

GO - Molecular functionⁱ

dihydrofolate reductase activity Source: UniProtKB-EC
NADP binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glycine biosynthetic process Source: InterPro
one-carbon metabolic process Source: UniProtKB-KW
tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	One-carbon metabolism
Ligand	NADP

Enzyme and pathway databases

BioCycⁱ	BSUB:BSU21810-MONOMER
UniPathwayⁱ	UPA00077; UER00158

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Dihydrofolate reductase (EC:1.5.1.3)
Gene namesⁱ	Name:dfrA Ordered Locus Names:BSU21810
Organismⁱ	Bacillus subtilis (strain 168)
Taxonomic identifierⁱ	224308 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis
Proteomesⁱ	UP000001570 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000186382	1 – 168	Dihydrofolate reductaseAdd BLAST		168

Proteomic databases

PaxDbⁱ	P11045
PRIDEⁱ	P11045

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	224308.Bsubs1_010100012011

STRINGⁱ

224308.Bsubs1_010100012011

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P11045
SMRⁱ	P11045
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 159	DHFRPROSITE-ProRule annotationAdd BLAST		159

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	5 – 7	Substrate bindingBy similarity		3

Sequence similaritiesⁱ

Belongs to the dihydrofolate reductase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4108YYV Bacteria COG0262 LUCA
HOGENOMⁱ	HOG000040233
InParanoidⁱ	P11045
KEGG Orthology (KO) More...KOⁱ	K00287
OMAⁱ	EECFVIG
PhylomeDBⁱ	P11045

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00209 DHFR, 1 hit
Gene3Dⁱ	3.40.430.10, 1 hit
InterProⁱ	View protein in InterPro IPR012259 DHFR IPR024072 DHFR-like_dom_sf IPR017925 DHFR_CS IPR001796 DHFR_dom
PANTHERⁱ	PTHR22778:SF16 PTHR22778:SF16, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00186 DHFR_1, 1 hit
PIRSFⁱ	PIRSF000194 DHFR, 1 hit
SUPFAMⁱ	SSF53597 SSF53597, 1 hit
PROSITEⁱ	View protein in PROSITE PS00075 DHFR_1, 1 hit PS51330 DHFR_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P11045-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MISFIFAMDA NRLIGKDNDL PWHLPNDLAY FKKITSGHSI IMGRKTFESI 
        60         70         80         90        100
GRPLPNRKNI VVTSAPDSEF QGCTVVSSLK DVLDICSGPE ECFVIGGAQL 
       110        120        130        140        150
YTDLFPYADR LYMTKIHHEF EGDRHFPEFD ESNWKLVSSE QGTKDEKNPY 
       160 
DYEFLMYEKK NSSKAGGF

Length:168

Mass (Da):19,176

Last modified:October 1, 1996 - v2

Checksum:ⁱ6E4D11D03F630A44

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	165	A → V in strain: MI112.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20012 Genomic DNA Translation: AAA22853.1 L77246 Genomic DNA Translation: AAA96635.1 AL009126 Genomic DNA Translation: CAB14099.1
PIRⁱ	JT0291 RDBSD
NCBI Reference Sequences More...RefSeqⁱ	NP_390064.1, NC_000964.3 WP_003230799.1, NZ_JNCM01000036.1

Genome annotation databases

EnsemblBacteriaⁱ	CAB14099; CAB14099; BSU21810
GeneIDⁱ	939091
KEGGⁱ	bsu:BSU21810
PATRICⁱ	fig\|224308.179.peg.2383

Protein	Similar proteins		Species	Score	Length
P11045	Dihydrofolate reductase		Bacillus subtilis subsp. subtilis str. SC-8		168
Dihydrofolate reductase		Bacillus subtilis BEST7613		168
Dihydrofolate reductase		BACIU		168

Protein	Similar proteins		Species	Score	Length
P11045	Dihydrofolate reductase		Bacillus subtilis subsp. subtilis str. SC-8		168
Dihydrofolate reductase		Bacillus subtilis BEST7613		168
Dihydrofolate reductase		BACIU		168
Dihydrofolate reductase		Bacillus sp. FMQ74		181
Dihydrofolate reductase		Bacillus sp. EGD-AK10		168
+49

Protein	Similar proteins		Species	Score	Length
P11045	Dihydrofolate reductase		Bacillus subtilis subsp. subtilis str. SC-8		168
Dihydrofolate reductase		Bacillus subtilis BEST7613		168
Dihydrofolate reductase		BACIU		168
Dihydrofolate reductase		Bacillus sp. FMQ74		181
UPI0008534229		Bacillus sp. F56		168
+501

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20012 Genomic DNA Translation: AAA22853.1 L77246 Genomic DNA Translation: AAA96635.1 AL009126 Genomic DNA Translation: CAB14099.1
PIRⁱ	JT0291 RDBSD
NCBI Reference Sequences More...RefSeqⁱ	NP_390064.1, NC_000964.3 WP_003230799.1, NZ_JNCM01000036.1

3D structure databases

ProteinModelPortalⁱ	P11045
SMRⁱ	P11045
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	224308.Bsubs1_010100012011

STRINGⁱ

224308.Bsubs1_010100012011

Proteomic databases

PaxDbⁱ	P11045
PRIDEⁱ	P11045

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CAB14099; CAB14099; BSU21810
GeneIDⁱ	939091
KEGGⁱ	bsu:BSU21810
PATRICⁱ	fig\|224308.179.peg.2383

Phylogenomic databases

eggNOGⁱ	ENOG4108YYV Bacteria COG0262 LUCA
HOGENOMⁱ	HOG000040233
InParanoidⁱ	P11045
KEGG Orthology (KO) More...KOⁱ	K00287
OMAⁱ	EECFVIG
PhylomeDBⁱ	P11045

Enzyme and pathway databases

UniPathwayⁱ	UPA00077; UER00158
BioCycⁱ	BSUB:BSU21810-MONOMER

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00209 DHFR, 1 hit
Gene3Dⁱ	3.40.430.10, 1 hit
InterProⁱ	View protein in InterPro IPR012259 DHFR IPR024072 DHFR-like_dom_sf IPR017925 DHFR_CS IPR001796 DHFR_dom
PANTHERⁱ	PTHR22778:SF16 PTHR22778:SF16, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00186 DHFR_1, 1 hit
PIRSFⁱ	PIRSF000194 DHFR, 1 hit
SUPFAMⁱ	SSF53597 SSF53597, 1 hit
PROSITEⁱ	View protein in PROSITE PS00075 DHFR_1, 1 hit PS51330 DHFR_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DYR_BACSU
Accessionⁱ	P11045Primary (citable) accession number: P11045
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	October 1, 1996
	Last modified:	May 23, 2018
	This is version 129 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

Bacillus subtilis
Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
PATHWAY comments
Index of metabolic and biosynthesis pathways
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P11045 (DYR_BACSU)

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Dihydrofolate reductase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolate biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

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Functionⁱ

Pathwayⁱ: tetrahydrofolate biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ