Reviewed, UniProtKB/Swiss-Prot Q2SZ52 (PUR9_BURTA)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC

Gene names

Name:	purH
Ordered Locus Names:	BTH_I1250

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	521 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 MF_00139 IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP 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 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 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	IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
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 – 521	521	Bifunctional purine biosynthesis protein purH HAMAP MF_00139		PRO_1000018863

Sequences

	Sequence		Length	Mass (Da)
	Q2SZ52-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: F5E9A0B7C592EC7C	FASTA	521	55,531
	10 20 30 40 50 60 MIKQALISVS DKTGIVDFAK ALSGLGVKLL STGGTAKLLA DAGLPVTEVA DYTGFPEMLD 70 80 90 100 110 120 GRVKTLHPKV HGGILARRDL PEHMQALEAH GIPTIDLLVV NLYPFVQTIA KDDCTLADAI 130 140 150 160 170 180 ENIDIGGPTM LRSAAKNHRD VTVVVDPADY AVVLDEMKAN GNTVGYKTNF RLATKVFAHT 190 200 210 220 230 240 AQYDGAITNY LTSLGDDLQH GSRNAYPATL NLAFDKVQDL RYGENPHQSA AFYRDVATPA 250 260 270 280 290 300 GALANYRQLQ GKELSYNNIA DSDAAWECVK TFDAPACVII KHANPCGVAV GADAGEAYAK 310 320 330 340 350 360 AFQTDPTSAF GGIIAFNREV DEVAAQAVAK QFVEVLIAPS FSEAAKQVFA AKQNVRLLEI 370 380 390 400 410 420 ALGEGHNAFD LKRVGGGLLV QSLDSKNVQP RELRVVTKRH PTPKEMDDLL FAWRVAKYVK 430 440 450 460 470 480 SNAIVFCGNG MTLGVGAGQM SRVDSARIAS IKAQNAGLTL AGSAVASDAF FPFRDGLDVV 490 500 510 520 VAAGATCVIQ PGGSVRDDEV IAAADEHNIA MVMTGVRHFR H

References

[1]

Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000086 Genomic DNA. Translation: ABC38801.1.
RefSeq	YP_441797.1.
3D structure databases
HSSP	HSSP built from PDB template 1M9N based on UniProtKB P31335.
SMR	Q2SZ52. Positions 2-521.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2SZ52.
Genome annotation databases
GeneID	3849634.
GenomeReviews	Gene locus BTH_I1250 in contig CP000086_GR.
KEGG	bte:BTH_I1250.
TIGR	BTH_I1250.
Phylogenomic databases
eggNOG	COG0138.
HOGENOM	HBG498048.
OMA	VVKHVKS.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_I1250-MONOMER.
Family and domain databases
HAMAP	MF_00139. PurH. [Tree]
InterPro	IPR002695. AICARFT_IMPCHas. IPR013982. AICARFT_IMPCHase_bienz. IPR011607. MGS. [Graphical view]
PANTHER	PTHR11692. AICARFT_IMPCHas. 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]
TIGRFAMs	TIGR00355. purH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_BURTA

Accession

Primary (citable) accession number: Q2SZ52

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 24, 2006
Last modified:	February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)