ID APT_HAEIN Reviewed; 180 AA.
AC P43856;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 29-MAY-2013, entry version 89.
DE RecName: Full=Adenine phosphoribosyltransferase;
DE Short=APRT;
DE EC=2.4.2.7;
GN Name=apt; OrderedLocusNames=HI_1230;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L42023; AAC22883.1; -; Genomic_DNA.
DR PIR; G64111; G64111.
DR RefSeq; NP_439386.1; NC_000907.1.
DR ProteinModelPortal; P43856; -.
DR SMR; P43856; 4-180.
DR STRING; 71421.HI1230; -.
DR EnsemblBacteria; AAC22883; AAC22883; HI_1230.
DR GeneID; 950707; -.
DR KEGG; hin:HI1230; -.
DR PATRIC; 20191139; VBIHaeInf48452_1282.
DR eggNOG; COG0503; -.
DR KO; K00759; -.
DR OMA; DYALEYG; -.
DR ProtClustDB; PRK02304; -.
DR UniPathway; UPA00588; UER00646.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:EC.
DR GO; GO:0006168; P:adenine salvage; IEA:InterPro.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1; -.
DR InterPro; IPR005764; Ade_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
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 Reference proteome; Transferase.
FT CHAIN 1 180 Adenine phosphoribosyltransferase.
FT /FTId=PRO_0000149391.
SQ SEQUENCE 180 AA; 19710 MW; 1E00D7165FE55ABA CRC64;
MTTQLDLIKS SIKSIPNYPK EGIIFRDITT LLEVPAAFKA TIDLIVEQYR DKGITKVLGT
ESRGFIFGAP VALALGLPFE LVRKPKKLPR ETISQSYQLE YGQDTLEMHV DAISEGDNVL
IIDDLLATGG TVEATVKLVQ RLGGAVKHAA FVINLPELGG EKRLNNLGVD CYTLVNFEGH
//
