P67539 (PUR9_BRUME) 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:	BMEI0233

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	538 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 – 538	538	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_0000192074

Sequences

	Sequence		Length	Mass (Da)
	P67539 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 099349D5160AC19F	FASTA	538	56,481
	10 20 30 40 50 60 MAVSSKHIPA PDLHRVRRAL LSVSDKTGLI DFAKALHANG VEILSTGGTA KSIAAAGIPV 70 80 90 100 110 120 KDVSEITGFP EIMDGRVKTL HPAVHGGLLA VRNDPEHVAA MEEHGIGGID LAVINLYPFE 130 140 150 160 170 180 EVRFKGGDYD TTVENIDIGG PAMIRASAKN HAYVATVVDP ADYADVVAEL EKHSGSLPLA 190 200 210 220 230 240 FRKKLAAKAF SRTAAYDAAI SNWFAEAIDE ETPTYRAVAG KLHSVMRYGE NPHQTAGFYL 250 260 270 280 290 300 TGEKRPGVAT ATQLQGKQLS YNNINDTDAA FELVAEFDPA RTAAVAIIKH ANPCGVAEAS 310 320 330 340 350 360 TIKEAYLKAL ACDPVSAFGG IVALNRTLDE EAAEEIVKTF TEVIIAPDAT EGAQAIVAAK 370 380 390 400 410 420 KNLRLLVTGG LPDPRAKGIA AKTVAGGLLV QSRDNGVVDD LDLKVVTKRA PTEAELNDLK 430 440 450 460 470 480 FAFRVGKHVK SNAIVYVKDG ATVGIGAGQM SRVDSARIAA RKAEDAAEAA GLAAPLTKGC 490 500 510 520 530 VVASDAFFPF ADGLLSAVEA GATAVIQPGG SMRDDEVIAA ADEHGIAMVM TGMRHFRH

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL51415.1.
PIR	AD3281.
RefSeq	NP_539151.1. NC_003317.1.
3D structure databases
ProteinModelPortal	P67539.
ModBase	Search...
Protein-protein interaction databases
STRING	224914.BMEI0233.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL51415; AAL51415; BMEI0233.
GeneID	1195945.
KEGG	bme:BMEI0233.
PATRIC	17802084. VBIBruMel146950_3359.
Organism-specific databases
CMR	Search...
Phylogenomic databases
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_BRUME

Accession

Primary (citable) accession number: P67539
Secondary accession number(s): Q8FYP8, Q8YJ53

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program