Q87KT0 (PUR9_VIBPA) 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:	VP2896

Organism

Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]

Taxonomic identifier

223926 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio harveyi group › Vibrio parahaemolyticus

Protein attributes

Sequence length	530 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 – 530	530	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_0000192146

Sequences

	Sequence		Length	Mass (Da)
	Q87KT0 [UniParc]. Last modified May 23, 2003. Version 1. Checksum: BC0242CD0F020B69	FASTA	530	57,322
	10 20 30 40 50 60 MNNARPIRRA LISVSDKTGI VEFAQALAER GVDILSTGGT ARLLAEQGIA VTEVSDYTGF 70 80 90 100 110 120 PEMMDGRVKT LHPKVHGGVL GRRGQDDDVM AKHGINPIDM VVVNLYPFAE TVAKDGCTLA 130 140 150 160 170 180 DAVENIDIGG PTMVRSAAKN HKDVTIVVNA SDYDRVIAEM DANDKSLTLE TRFDLAIAAF 190 200 210 220 230 240 EHTAAYDGMI ANYFGTMVPS YGENKEGDEE SKFPRTFNQQ FEKKQDMRYG ENSHQAAAFY 250 260 270 280 290 300 VEANPQEASV STARQIQGKA LSYNNIADTD AALECVKEFN EPACVIVKHA NPCGVALGKD 310 320 330 340 350 360 ILEAYNRAYQ TDPTSAFGGI IAFNQELDAE TASAIVERQF VEVIIAPSVS AEAIEVVAAK 370 380 390 400 410 420 KNVRLLECGE WTTKTTGFDV KRVNGGLLVQ DRDQGMVSLD DLKVVSKRQP TEEELKDALF 430 440 450 460 470 480 CWKVAKYVKS NAIVYAKGDM TIGVGAGQMS RVYSAKIAGI KAADEGLEVA GSVMASDAFF 490 500 510 520 530 PFRDGIDAAA EAGIKCVIQP GGSMRDDEVI AAADEHGMAM IFTGMRHFRH

References

[1]

"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000031 Genomic DNA. Translation: BAC61159.1.
RefSeq	NP_799275.1. NC_004603.1.
3D structure databases
ProteinModelPortal	Q87KT0.
ModBase	Search...
Protein-protein interaction databases
STRING	223926.VP2896.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC61159; BAC61159; BAC61159.
GeneID	1190471.
KEGG	vpa:VP2896.
PATRIC	20144040. VBIVibPar50997_2787.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0138.
HOGENOM	HOG000230372.
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_VIBPA

Accession

Primary (citable) accession number: Q87KT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 23, 2003
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program