Reviewed, UniProtKB/Swiss-Prot A0LUK1 (APT_ACIC1)

Names and origin

Protein names

Recommended name:
    Adenine phosphoribosyltransferase
      Short name=APRT
    EC=2.4.2.7

Gene names

Name:	apt
Ordered Locus Names:	Acel_1339

Organism

Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]

Taxonomic identifier

351607 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis By similarity.
Catalytic activity	AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00004
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. HAMAP MF_00004
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	adenine salvage Inferred from electronic annotation. Source: HAMAP purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	adenine phosphoribosyltransferase 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 – 177	177	Adenine phosphoribosyltransferase HAMAP MF_00004		PRO_0000321329

Sequences

	Sequence		Length	Mass (Da)
	A0LUK1-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: B1580AD5EC84AEE4	FASTA	177	18,718
	10 20 30 40 50 60 MPPADIGELV AAHIRDIPDY PSPGIVFKDI TPLLAEPAVF AAVVDALVRD YQHGTVDKVV 70 80 90 100 110 120 GIEARGFIVA APVAYHLGAG FVPMRKKGKL PYRTLETSYA LEYGTATIEV HVDAFRPGDR 130 140 150 160 170 VLVVDDVLAT GGTAAAALEL IDQASAKAVG LSFLIELSAL GGRSRLPASM VRSLLRV

References

[1]

"Complete sequence of Acidothermus cellulolyticus 11B." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000481 Genomic DNA. Translation: ABK53111.1.
RefSeq	YP_873097.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0LUK1.
Genome annotation databases
GeneID	4484764.
GenomeReviews	Gene locus Acel_1339 in contig CP000481_GR.
KEGG	ace:Acel_1339.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	KPGKLPA.
Family and domain databases
HAMAP	MF_00004. [Tree]
InterPro	IPR005764. Ade_phspho_trans. IPR002375. Pr/py_Pribosyl_transf_CS. IPR000836. PRibTrfase. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01090. apt. 1 hit.
PROSITE	PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APT_ACIC1

Accession

Primary (citable) accession number: A0LUK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	December 12, 2006
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)