P0DD60 (PUR9_STRP3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
   EC=2.1.2.3
   Alternative name(s):
   AICAR transformylase
2. IMP cyclohydrolase
   EC=3.5.4.10
   Alternative name(s):
   ATIC
   IMP synthase
   Inosinicase

Gene names

Name:	purH
Ordered Locus Names:	SpyM3_0024

Organism

Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) [Complete proteome] [HAMAP]

Taxonomic identifier

198466 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pyogenes › Streptococcus pyogenes serotype M3

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139 IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139 Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
Domain	The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139
Sequence similarities	Belongs to the PurH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylaminoimidazolecarboxamide formyltransferase 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 – 515	515	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_0000192136

Sequences

	Sequence		Length	Mass (Da)
	P0DD60 [UniParc]. Last modified July 27, 2011. Version 1. Checksum: 58C11340BBB97049	FASTA	515	56,217
	10 20 30 40 50 60 MTKRALISVS DKSGIVDFAK ELKNLGWDII STGGTKVALD NAGVETIAID DVTGFPEMMD 70 80 90 100 110 120 GRVKTLHPNI HGGLLARRDA DSHLQAAKDN NIELIDLVVV NLYPFKETIL RPDITYDLAV 130 140 150 160 170 180 ENIDIGGPSM LRSAAKNHAS VTVVVDPADY ATVLGELADA GQTTFETRQR LAAKVFRHTA 190 200 210 220 230 240 AYDALIAEYF TTQVGEAKPE KLTITYDLKQ AMRYGENPQQ DADFYQKALP IDYSIASAKQ 250 260 270 280 290 300 LNGKELSFNN IRDADAAIRI IRDFKDRPTV VVLKHMNPCG IGQADDIETA WDYAYEADPV 310 320 330 340 350 360 SIFGGIVVLN REVDAATAKK MHPIFLEIII APSYSEEALA ILTNKKKNLR ILELPFDAQA 370 380 390 400 410 420 ASEVEAEYTG VVGGLLVQNQ DVVAENPSDW QVVTDRQPTE QEATALEFAW KAIKYVKSNG 430 440 450 460 470 480 IIITNDHMTL GLGAGQTNRV GSVKIAIEQA KDHLDGAVLA SDAFFPFADN IEEIAAAGIK 490 500 510 AIIQPGGSVR DQDSIDAANK HGLTMIFTGV RHFRH

References

[1]

"Genome sequence of a serotype M3 strain of group A Streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence." Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M. Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-595 / MGAS315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014074 Genomic DNA. Translation: AAM78631.1.
RefSeq	NP_663828.1. NC_004070.1.
3D structure databases
ProteinModelPortal	P0DD60.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM78631; AAM78631; SpyM3_0024.
GeneID	1008338.
KEGG	spg:SpyM3_0024.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000230373.
KO	K00602.
OMA	DLLFAWK.
Enzyme and pathway databases
UniPathway	UPA00074; UER00133. UPA00074; UER00135.
Family and domain databases
Gene3D	3.40.140.20. 2 hits. 3.40.50.1380. 1 hit.
HAMAP	MF_00139. PurH.
InterPro	IPR024051. AICAR_Tfase_dom. IPR002695. AICARFT_IMPCHas. IPR016193. Cytidine_deaminase-like. IPR011607. MGS-like_dom. [Graphical view]
PANTHER	PTHR11692. PTHR11692. 1 hit.
Pfam	PF01808. AICARFT_IMPCHas. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PIRSF	PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMART	SM00798. AICARFT_IMPCHas. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit. SSF52335. MGS-like_dom. 1 hit.
TIGRFAMs	TIGR00355. purH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_STRP3

Accession

Primary (citable) accession number: P0DD60
Secondary accession number(s): Q8K8Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program