Q38XW3 (PUR9_LACSS) 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:	LCA_0662

Organism

Lactobacillus sakei subsp. sakei (strain 23K) [Complete proteome] [HAMAP]

Taxonomic identifier

314315 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus sakei › Lactobacillus sakei subsp. sakei

Protein attributes

Sequence length	510 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 – 510	510	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_1000018903

Sequences

	Sequence		Length	Mass (Da)
	Q38XW3 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 2A9F090BB903CC6B	FASTA	510	55,410
	10 20 30 40 50 60 MKRALISVSD KTGIVAFAQG LVAADFEIIS TGGTFSVLEK AGVPVTPIDE VTHFPEMLDG 70 80 90 100 110 120 RVKTLHPNIH GGLLAKRDEP THMAALAEHE IAPIDLVCVN LYPFKETIQK PEITQEQAIE 130 140 150 160 170 180 QIDIGGPSML RSAAKNFKSV YVVVDQADYD ETLAQLQQDD VTYRRHLAAK AFRHTAAYDS 190 200 210 220 230 240 LIAGYLSDAD AVEFPEKLSL TYDFKQALRY GENAHQKAAF YQSALPSAFS IAAAHQLHGK 250 260 270 280 290 300 ELSYNNIKDA DAAIKVAAEF SEPCVVAMKH MNPCGVGLGT TIYDAWQKAF AADSVSIFGG 310 320 330 340 350 360 IIALNREVDV QTANALHELF LEIVIAPSFA PEALAILEKK KNIRLMTLDF EQAAKADRFE 370 380 390 400 410 420 TVSVLGGLLV QERDRLTDQA SELKTVTTKA PTEDEKEALL FAQRVVKHVK SNAIVVATKG 430 440 450 460 470 480 QTLGVGAGQM NRVGSVKIAL EQALANGMQA PFVLASDAFF PMDDSVAYAA EHGITAIIQP 490 500 510 GGSIKDQDSI DMANQKGVSM VFTNRRHFKH

References

[1]

"The complete genome sequence of the meat-borne lactic acid bacterium Lactobacillus sakei 23K." Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V., Zagorec M. Nat. Biotechnol. 23:1527-1533(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 23K.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR936503 Genomic DNA. Translation: CAI54966.1.
RefSeq	YP_395277.1. NC_007576.1.
3D structure databases
HSSP	HSSP built from PDB template 1M9N based on UniProtKB P31335.
ProteinModelPortal	Q38XW3.
ModBase	Search...
Protein-protein interaction databases
STRING	314315.LSA0662.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAI54966; CAI54966; LCA_0662.
GeneID	3777559.
KEGG	lsa:LSA0662.
PATRIC	22274144. VBILacSak116432_0640.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0138.
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_LACSS

Accession

Primary (citable) accession number: Q38XW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 22, 2005
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program