Q8NS21 (PUR9_CORGL) 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:	Cgl0861, cg0984

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 Reference proteome
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 – 520	520	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_0000192089

Sequences

	Sequence		Length	Mass (Da)
	Q8NS21 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 8A3A80B3AF18AAB7	FASTA	520	55,760
	10 20 30 40 50 60 MSDDRKAIKR ALISVYDKTG LEDLAQALHR ENVEIVSTGS TAAKIAELGI PVTPVEELTG 70 80 90 100 110 120 FPECLEGRVK TLHPKVHAGI LADTRKEDHL RQLKELEVAP FQLVVVNLYP FAETVASGAD 130 140 150 160 170 180 FDACVEQIDI GGPSMVRAAA KNHPSVAVVV SPNRYEDVQE ALKTGGFSRA ERTKLAAEAF 190 200 210 220 230 240 RHTATYDVTV ATWMSEQLAA EDSETEFPGW IGTTNTLSRS LRYGENPHQS AALYVGNTRG 250 260 270 280 290 300 LAQAKQFHGK EMSYNNYTDS DAAWRAAWDH ERPCVAIIKH ANPCGIAVSD ESIAAAHREA 310 320 330 340 350 360 HACDSVSAFG GVIASNREVS VEMANQVAEI FTEVIIAPSY EEGAVEILSQ KKNIRILQAE 370 380 390 400 410 420 APVRKGFESR EISGGLLVQE RDLIHAEGDN SANWTLAAGS AVSPEVLKDL EFAWTAVRSV 430 440 450 460 470 480 KSNAILLAKN GATVGVGMGQ VNRVDSARLA VDRAGAERAT GSVAASDAFF PFADGFEVLA 490 500 510 520 EAGITAVVQP GGSIRDNEVI EAANKAGVTM YLTGARHFAH

References

[1]

"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB98254.1. BX927150 Genomic DNA. Translation: CAF19567.1.
RefSeq	NP_600090.1. NC_003450.3. YP_225153.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NS21.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg0984.
2D gel databases
World-2DPAGE	0001:Q8NS21.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB98254; BAB98254; BAB98254. CAF19567; CAF19567; cg0984.
GeneID	1018856. 3343365.
KEGG	cgb:cg0984. cgl:NCgl0827.
PATRIC	21493774. VBICorGlu203724_0846.
Phylogenomic databases
eggNOG	COG0138.
HOGENOM	HOG000230373.
KO	K00602.
OMA	DLLFAWK.
ProtClustDB	PRK00881.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-857-MONOMER.
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_CORGL

Accession

Primary (citable) accession number: Q8NS21

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program