P67545 (PUR9_STRA3) 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:	gbs0029

Organism

Streptococcus agalactiae serotype III (strain NEM316) [Complete proteome] [HAMAP]

Taxonomic identifier

211110 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus agalactiae › Streptococcus agalactiae serogroup III

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_0000192130

Sequences

	Sequence		Length	Mass (Da)
	P67545 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 763688642FA48CC6	FASTA	515	56,084
	10 20 30 40 50 60 MTKRALISVS DKSGIIDFAK ELKNLGWDII STGGTKVALD DAGVETIAID DVTGFPEMMD 70 80 90 100 110 120 GRVKTLHPNI HGGLLARRDA DSHLQAAKDN NIELIDLVVV NLYPFKETIL RPDVTYDLAV 130 140 150 160 170 180 ENIDIGGPSM LRSAAKNHAS VTVVVDSADY ATVLGELADA SQTTFKTRQR LAAKAFRHTA 190 200 210 220 230 240 AYDALIAEYF TAQVGEAKPE KLTITYDLKQ AMRYGENPQQ DADFYQKALP TDYSIASAKQ 250 260 270 280 290 300 LNGKELSFNN IRDADAAIRI IRDFKDSPTV VALKHMNPCG IGQADDIETA WDYAYEADPV 310 320 330 340 350 360 SIFGGIVVLN REVDAATAEK 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 DQESIDAANK HGLTMIFTGV RHFRH

References

[1]

"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease." Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F. Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NEM316.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL766843 Genomic DNA. Translation: CAD45674.1.
RefSeq	NP_734499.1. NC_004368.1.
3D structure databases
ProteinModelPortal	P67545.
ModBase	Search...
Protein-protein interaction databases
STRING	211110.gbs0029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD45674; CAD45674; CAD45674.
GeneID	1031413.
KEGG	san:gbs0029.
PATRIC	19635761. VBIStrAga3577_0029.
Organism-specific databases
GenoList	gbs0029.
CMR	Search...
Phylogenomic databases
eggNOG	COG0138.
HOGENOM	HOG000230373.
KO	K00602.
OMA	DLLFAWK.
ProtClustDB	PRK00881.
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_STRA3

Accession

Primary (citable) accession number: P67545
Secondary accession number(s): Q8E2F8, Q8E7W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program