Q5XCA8 (DHPS_STRP6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydropteroate synthase
Short name=DHPS
EC=2.5.1.15

Alternative name(s):
Dihydropteroate pyrophosphorylase

Gene names

Name:	folP
Ordered Locus Names:	M6_Spy0820

Organism

Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) [Complete proteome] [HAMAP]

Taxonomic identifier

286636 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pyogenes › Streptococcus pyogenes serotype M6

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide By similarity.
Catalytic activity	(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
Cofactor	Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate By similarity.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Subunit structure	Homodimer or homotrimer By similarity.
Sequence similarities	Belongs to the DHPS family. Contains 1 pterin-binding domain.

Ontologies

Keywords
Biological process	Antibiotic resistance Folate biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	dihydropteroate synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 266	266	Dihydropteroate synthase		PRO_0000168235
Regions
	Domain	12 – 260	249	Pterin-binding
	Region	59 – 60	2	Substrate binding By similarity
Sites
	Metal binding	19	1	Magnesium By similarity
	Binding site	27	1	Substrate By similarity
	Binding site	93	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	176	1	Substrate By similarity
	Binding site	212	1	Substrate By similarity
	Binding site	248	1	Substrate By similarity
	Binding site	250	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5XCA8 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: B143DBBBD45A78F0	FASTA	266	28,686
	10 20 30 40 50 60 MKIGKFVIEG NAAIMGILNV TPDSFSDGGS YTTVQKALDH VEQMIADGAK IIDVGGESTR 70 80 90 100 110 120 PGCQFVSATD EIDRVVPVIK AIKENYDILI SIDTYKTETA RAALEAGADI LNDVWAGLYD 130 140 150 160 170 180 GQMFALAAEY DAPIILMHNQ DEEVYQEVTQ DVCDFLGNRA QAALDAGVPK NNIWIDPGFG 190 200 210 220 230 240 FAKSVQQNME LLKGLDRVCQ LGYPVLFGIS RKRVVDALLG GNTKAKERDG ATAALSAYAL 250 260 GKGCQIVRVH DVKANQDIVA VLSQLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain." Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M. J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-946 / MGAS10394.
[2]	"Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins." Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A. Submitted (MAY-2000) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-12; 37-50; 81-96; 160-170; 214-224 AND 229-242. Strain: JRS4 / Serotype M6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000003 Genomic DNA. Translation: AAT86955.1.
RefSeq	YP_060138.1. NC_006086.1.
3D structure databases
ProteinModelPortal	Q5XCA8.
ModBase	Search...
Protein-protein interaction databases
STRING	286636.M6_Spy0820.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT86955; AAT86955; M6_Spy0820.
GeneID	2940918.
KEGG	spa:M6_Spy0820.
PATRIC	19723806. VBIStrPyo30273_0848.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0294.
HOGENOM	HOG000217509.
KO	K00796.
OMA	QHWRGWL.
ProtClustDB	CLSK797490.
Enzyme and pathway databases
UniPathway	UPA00077; UER00156.
Family and domain databases
Gene3D	3.20.20.20. 1 hit.
InterPro	IPR006390. DHP_synth. IPR011005. Dihydropteroate_synth-like. IPR000489. Pterin-binding. [Graphical view]
Pfam	PF00809. Pterin_bind. 1 hit. [Graphical view]
SUPFAM	SSF51717. DHP_synth_like. 1 hit.
TIGRFAMs	TIGR01496. DHPS. 1 hit.
PROSITE	PS00792. DHPS_1. 1 hit. PS00793. DHPS_2. 1 hit. PS50972. PTERIN_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHPS_STRP6

Accession

Primary (citable) accession number: Q5XCA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	November 23, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program