Reviewed, UniProtKB/Swiss-Prot Q2K5T4 (APT1_RHIEC)

Names and origin

Protein names

Recommended name:
    Adenine phosphoribosyltransferase 1
      Short name=APRT 1
    EC=2.4.2.7

Gene names

Name:	apt1
Ordered Locus Names:	RHE_CH03035

Organism

Rhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]

Taxonomic identifier

347834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium

Protein attributes

Sequence length	180 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 – 180	180	Adenine phosphoribosyltransferase 1 HAMAP MF_00004		PRO_0000334715

Sequences

	Sequence		Length	Mass (Da)
	Q2K5T4-1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: D098E64A638F310D	FASTA	180	19,329
	10 20 30 40 50 60 MGNTISELAA SIRSIPDYPN PGIIFRDITT LLGNPRAFRR AVDELVQPYA GTKVDKIAGM 70 80 90 100 110 120 EARGFILGGA VAHQLSSGFV PIRKKGKLPH DTVRIAYSLE YGVDEMEMHR DAVQPGEKVI 130 140 150 160 170 180 LVDDLIATGG TAVGATQLLR QIGAEVVGAC FVIDLPDLGG RRKLEELGVV VHTLVEFSGH

References

[1]

"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons." Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G. Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed: 16505379] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000133 Genomic DNA. Translation: ABC91802.1. Different initiation.
RefSeq	YP_470529.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2K5T4.
Genome annotation databases
GeneID	3893309.
GenomeReviews	Gene locus RHE_CH03035 in contig CP000133_GR.
KEGG	ret:RHE_CH03035.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2K5T4.
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

APT1_RHIEC

Accession

Primary (citable) accession number: Q2K5T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	September 1, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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