Amidophosphoribosyltransferase precursor - Mycobacterium tuberculosis

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P65829 (PUR1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. History...

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

Documents (2) |

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:
Amidophosphoribosyltransferase
Short name=ATase
EC=2.4.2.14

Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPATase

Gene names

Name:	purF
Ordered Locus Names:	Rv0808, MT0829
ORF Names:	MTCY07H7A.01c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H₂O.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW growth Inferred from mutant phenotype. Source: MTBBASE nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 34

By similarity

PRO_0000029257

Chain

35 – 527

493

Amidophosphoribosyltransferase

PRO_0000029258

Regions

Domain

35 – 261

227

Glutamine amidotransferase type-2

Sites

Active site

For GATase activity By similarity

Metal binding

276

Iron-sulfur (4Fe-4S) By similarity

Metal binding

323

Magnesium By similarity

Metal binding

385

Magnesium By similarity

Metal binding

386

Magnesium By similarity

Metal binding

422

Iron-sulfur (4Fe-4S) By similarity

Metal binding

478

Iron-sulfur (4Fe-4S) By similarity

Metal binding

481

Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P65829 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: A2FE9D1DD08FA572
Show »

FASTA

527

56,162

        10         20         30         40         50         60 
MAVDSDYVTD RAAGSRQTVT GQQPEQDLNS PREECGVFGV WAPGEDVAKL TYYGLYALQH 

        70         80         90        100        110        120 
RGQEAAGIAV ADGSQVLVFK DLGLVSQVFD EQTLAAMQGH VAIGHCRYST TGDTTWENAQ 

       130        140        150        160        170        180 
PVFRNTAAGT GVALGHNGNL VNAAALAARA RDAGLIATRC PAPATTDSDI LGALLAHGAA 

       190        200        210        220        230        240 
DSTLEQAALD LLPTVRGAFC LTFMDENTLY ACRDPYGVRP LSLGRLDRGW VVASETAALD 

       250        260        270        280        290        300 
IVGASFVRDI EPGELLAIDA DGVRSTRFAN PTPKGCVFEY VYLARPDSTI AGRSVHAARV 

       310        320        330        340        350        360 
EIGRRLAREC PVEADLVIGV PESGTPAAVG YAQESGVPYG QGLMKNAYVG RTFIQPSQTI 

       370        380        390        400        410        420 
RQLGIRLKLN PLKEVIRGKR LIVVDDSIVR GNTQRALVRM LREAGAVELH VRIASPPVKW 

       430        440        450        460        470        480 
PCFYGIDFPS PAELIANAVE NEDEMLEAVR HAIGADTLGY ISLRGMVAAS EQPTSRLCTA 

       490        500        510        520 
CFDGKYPIEL PRETALGKNV IEHMLANAAR GAALGELAAD DEVPVGR

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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	BX842574 Genomic DNA. Translation: CAB09103.1. AE000516 Genomic DNA. Translation: AAK45071.1.
PIR	A70537.
RefSeq	NP_215323.1. NC_000962.2. NP_335257.1. NC_002755.2.
3D structure databases
ProteinModelPortal	P65829.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000000558; EBMYCP00000000558; EBMYCG00000000558. EBMYCT00000071613; EBMYCP00000069672; EBMYCG00000071608.
GeneID	885085. 926132.
GenomeReviews	Gene locus MT0829 in contig AE000516_GR. Gene locus Rv0808 in contig AL123456_GR.
KEGG	mtc:MT0829. mtu:Rv0808.
PATRIC	18123562. VBIMycTub22151_0909.
TIGR	MT0829.
Organism-specific databases
TubercuList	Rv0808.
Phylogenomic databases
GeneTree	EBGT00050000016850.
HOGENOM	HBG392416.
OMA	VWAPGEE.
PhylomeDB	P65829.
ProtClustDB	PRK07847.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. IPR000836. PRibTrfase. [Graphical view]
KO	K00764.
PANTHER	PTHR11907. Amd_phspho_trans. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. PF00156. Pribosyltran. 1 hit. [Graphical view]
PIRSF	PIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMs	TIGR01134. PurF. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR1_MYCTU

Accession

Primary (citable) accession number: P65829
Secondary accession number(s): O06626

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 56 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

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

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

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