A5VHU2 (PUR9_LACRD) 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:	Lreu_0144

Organism

Lactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]

Taxonomic identifier

557436 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus reuteri

Protein attributes

Sequence length	512 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 – 512	512	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_1000057899

Sequences

	Sequence		Length	Mass (Da)
	A5VHU2 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: ECEC7A2970255506	FASTA	512	57,033
	10 20 30 40 50 60 MKRALVSVSD KQNLVPFVKG LVENGFEIIS TGGTKRVLDE AGIETIGIED VTHFPEILDG 70 80 90 100 110 120 RVKTLNPYVH GGLLARRNLP EHMATLEKLN ITPIDLVCVN LYPFKETIEK PGVEIADAIE 130 140 150 160 170 180 NIDIGGPSMV RSAAKNYHDV TIVVDQADYD EVLAQIKEDG ETSLATRARL AAKAFRHTAA 190 200 210 220 230 240 YDSLISQYLT KQTGLEDPEK LTLSWDLKET MRYGENSHQK AWLYEDALPK AFSVLQAKQL 250 260 270 280 290 300 HGKKLSYNNI KDADEALRCI REFDEPTVVA MKHMNPCGIG RGDSLVQAWD RAYEADPVSI 310 320 330 340 350 360 FGGVIALNRQ VDLVTAEKMH KIFLEIVIAP GFDDDAFELL AKKKNIRLLT LDFSKKDEPT 370 380 390 400 410 420 KHEVVSVMGG MLLQEQDMLK EDYHDWQCVT EKQPTEEQLK TLMFAWKAVK HAKSNAIVLA 430 440 450 460 470 480 NDERTLGVGE GQPNRIDSLK IAVKHAGEAI DDRTVMASDA FFPFGDCVEY AGQNGIKAIV 490 500 510 QPGGSVRDQE SIEMANKYGI AMVTTGIRHF RH

References

[1]

"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri." Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. , Ivanova N., Kyrpides N.C., Walter J. PLoS Genet. 7:E1001314-E1001314(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 20016.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000705 Genomic DNA. Translation: ABQ82416.1.
RefSeq	YP_001270753.1. NC_009513.1.
3D structure databases
ProteinModelPortal	A5VHU2.
ModBase	Search...
Protein-protein interaction databases
STRING	557436.Lreu_0144.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ82416; ABQ82416; Lreu_0144.
GeneID	5189507.
KEGG	lre:Lreu_0144.
PATRIC	22253352. VBILacReu87937_0150.
Organism-specific databases
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_LACRD

Accession

Primary (citable) accession number: A5VHU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program