Bifunctional purine biosynthesis protein PurH

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P67541 (PUR9_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

Phosphoribosylaminoimidazolecarboxamide formyltransferase
EC=2.1.2.3
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase
EC=3.5.4.10
Alternative name(s):
ATIC
IMP synthase
Inosinicase

Gene names

Name:	purH
Ordered Locus Names:	Rv0957, MT0984
ORF Names:	MTCY10D7.17c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	523 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 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	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

Bifunctional purine biosynthesis protein PurH HAMAP MF_00139

PRO_0000192106

Sequences

Sequence

Length

Mass (Da)

Tools

P67541 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 5A78C034101019C7
Show »

FASTA

523

55,026

        10         20         30         40         50         60 
MSTDDGRRPI RRALISVYDK TGLVDLAQGL SAAGVEIIST GSTAKTIADT GIPVTPVEQL 

        70         80         90        100        110        120 
TGFPEVLDGR VKTLHPRVHA GLLADLRKSE HAAALEQLGI EAFELVVVNL YPFSQTVESG 

       130        140        150        160        170        180 
ASVDDCVEQI DIGGPAMVRA AAKNHPSAAV VTDPLGYHGV LAALRAGGFT LAERKRLASL 

       190        200        210        220        230        240 
AFQHIAEYDI AVASWMQQTL APEHPVAAFP QWFGRSWRRV AMLRYGENPH QQAALYGDPT 

       250        260        270        280        290        300 
AWPGLAQAEQ LHGKDMSYNN FTDADAAWRA AFDHEQTCVA IIKHANPCGI AISSVSVADA 

       310        320        330        340        350        360 
HRKAHECDPL SAYGGVIAAN TEVSVEMAEY VSTIFTEVIV APGYAPGALD VLARKKNIRV 

       370        380        390        400        410        420 
LVAAEPLAGG SELRPISGGL LIQQSDQLDA HGDNPANWTL ATGSPADPAT LTDLVFAWRA 

       430        440        450        460        470        480 
CRAVKSNAIV IAADGATVGV GMGQVNRVDA ARLAVERGGE RVRGAVAASD AFFPFPDGLE 

       490        500        510        520 
TLAAAGVTAV VHPGGSVRDE EVTEAAAKAG VTLYLTGARH FAH

« Hide

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842575 Genomic DNA. Translation: CAB01993.1.
AE000516 Genomic DNA. Translation: AAK45232.1.

PIR

C70717.

RefSeq

NP_215472.1. NC_000962.2.
NP_335418.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ZZM	X-ray	2.20	A/B	1-523	[»]
4A1O	X-ray	2.48	A/B	1-523	[»]

ProteinModelPortal

P67541.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000000576; EBMYCP00000000576; EBMYCG00000000576.
EBMYCT00000070747; EBMYCP00000068806; EBMYCG00000070742.

GeneID

885406.
926376.

GenomeReviews

Gene locus MT0984 in contig AE000516_GR.
Gene locus Rv0957 in contig AL123456_GR.

KEGG

mtc:MT0984.
mtu:Rv0957.

PATRIC

18123908. VBIMycTub22151_1077.

TIGR

MT0984.

Organism-specific databases

TubercuList

Rv0957.

Phylogenomic databases

GeneTree

EBGT00050000017138.

HOGENOM

HBG498048.

OMA

FTGTRHF.

PhylomeDB

P67541.

ProtClustDB

PRK00881.

Family and domain databases

HAMAP

MF_00139. PurH.
[Tree]

InterPro

IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]

Gene3D

G3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits.
G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.

K00602.

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]

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_MYCTU

Accession

Primary (citable) accession number: P67541
Secondary accession number(s): P71553

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents