Amidophosphoribosyltransferase precursor - Mycobacterium leprae (strain TN)

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Q50028 (PUR1_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. 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:	ML2206
ORF Names:	MLCB5.38

Organism

Mycobacterium leprae (strain TN) [Complete proteome] [HAMAP]

Taxonomic identifier

272631 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	556 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
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro
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 – 57

By similarity

PRO_0000029255

Chain

58 – 556

499

Amidophosphoribosyltransferase

PRO_0000029256

Regions

Domain

58 – 284

227

Glutamine amidotransferase type-2

Sites

Active site

For GATase activity By similarity

Metal binding

299

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

Metal binding

346

Magnesium By similarity

Metal binding

408

Magnesium By similarity

Metal binding

409

Magnesium By similarity

Metal binding

445

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

Metal binding

501

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

Metal binding

504

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q50028 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E0CF4D278302FDCE
Show »

FASTA

556

59,540

        10         20         30         40         50         60 
MCLAVGVGVR APKHVPQIRR LGRAGRRLRC VTNCALGSCP IVTVQQPGRD FSSPREECGV 

        70         80         90        100        110        120 
FGVWAPGELV AKLTYFGLYA LQHRGQEAAG IAVADGSQVL VFKDLGLVSQ VFDEQTLAAM 

       130        140        150        160        170        180 
EGHVAIGHCR YSTTGDTTWE NAQPVFRNIA AGSGVALGHN GNLVNTAELA ARARDAGLIA 

       190        200        210        220        230        240 
KRCPAPATTD SDILGALLAH GAADSTLEQA ALELLPTVRG AFCLTFMDEN TLYACRDPYG 

       250        260        270        280        290        300 
VRPLSLGRLD RGWVVASETA GLDIVGASFV RDIEPGELLA IDADGVRSTR FANPTPKGCV 

       310        320        330        340        350        360 
FEYVYLARPD STLAGRSVHG TRVEIGRRLA RECPVEADLV IGVPESGTPA AVGYAQESGI 

       370        380        390        400        410        420 
SYGQGLMKNA YVGRTFIQPS QTIRQLGIRL KLNPLKEVIR GKRLIVVDDS VVRGNTQRAL 

       430        440        450        460        470        480 
VRMLREAGAV ELHVRIASPP VKWPCFYGID FPSPAELIAN VVADEEEMLE AVRQGIGADT 

       490        500        510        520        530        540 
LGYISLRGMI AASEQPASRL CYACFDGRYP IELPSEAMLG KNVIEHMLAN AARGAGLRDL 

       550 
AADQVPVDAD ENCVWR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G. Nature 409:1007-1011(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15182 Genomic DNA. Translation: AAA62988.1. Z95151 Genomic DNA. Translation: CAB08437.1. AL583924 Genomic DNA. Translation: CAC31161.1.
PIR	A87185.
RefSeq	NP_302447.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q50028.
ModBase	Search...
Protein-protein interaction databases
STRING	272631.ML2206.
Protein family/group databases
MEROPS	C44.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC31161; CAC31161; CAC31161.
GeneID	908827.
KEGG	mle:ML2206.
PATRIC	18058519. VBIMycLep78757_4178.
Organism-specific databases
Leproma	ML2206.
CMR	Search...
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HOG000033688.
KO	K00764.
OMA	GIPFELG.
ProtClustDB	PRK07847.
Enzyme and pathway databases
UniPathway	UPA00074; UER00124.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	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_MYCLE

Accession

Primary (citable) accession number: Q50028
Secondary accession number(s): O05762

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 99 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

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents