ID   APT_SULDN               Reviewed;         182 AA.
AC   Q30RI5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   29-APR-2008, entry version 26.
DE   Adenine phosphoribosyltransferase (EC 2.4.2.7) (APRT).
GN   Name=apt; OrderedLocusNames=Suden_1118;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251)
OS   (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J.,
RA   Hemp J., Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S.,
RA   Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K.,
RA   Diaz E., Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A.,
RA   Long A., Mobberley J.M., Pantry S.N., Pazder G., Peterson S.,
RA   Quintanilla J.D., Sprinkle R., Stephens J., Thomas P., Vaughn R.,
RA   Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
CC   -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation
CC       of AMP, that is energically less costly than de novo synthesis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha-
CC       D-ribose 1-diphosphate.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from adenine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000153; ABB44396.1; -; Genomic_DNA.
DR   RefSeq; YP_393631.1; -.
DR   GeneID; 3763667; -.
DR   GenomeReviews; CP000153_GR; Suden_1118.
DR   KEGG; tdn:Tmden_1118; -.
DR   NMPDR; fig|326298.3.peg.1950; -.
DR   GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006168; P:adenine salvage; IEA:HAMAP.
DR   HAMAP; MF_00004; -; 1.
DR   InterPro; IPR005764; Ade_phspho_trans.
DR   InterPro; IPR002375; Pr/py_Pribosyl_transf_CS.
DR   InterPro; IPR000836; PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   TIGRFAMs; TIGR01090; apt; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage;
KW   Transferase.
FT   CHAIN         1    182       Adenine phosphoribosyltransferase.
FT                                /FTId=PRO_0000321414.
SQ   SEQUENCE   182 AA;  20042 MW;  5286AAFF3BD192E2 CRC64;
     MTLSNTERAI IESAIRDIKD FPKPGIVFKD ITTLLNNGKA FGVTMNHLYE KYKEYNLDYI
     AGIDARGFIF GAALAQMLGV GFVPIRKKGK LPYTTISEKY SLEYGFDEVE IHLDAFSAIP
     NARVLLVDDL IATGGTAAAS VKLINQAGAL CVEACFILCL SFLDGYKKLQ ELTEVYSLVE
     VK
//