ID B6HKJ3_PENRW Unreviewed; 202 AA.
AC B6HKJ3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN ORFNames=Pc21g11750 {ECO:0000313|EMBL:CAP96072.1}, PCH_Pc21g11750
GN {ECO:0000313|EMBL:CAP96072.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP96072.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP96072.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000256|ARBA:ARBA00003968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000868};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000256|ARBA:ARBA00008391}.
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DR EMBL; AM920436; CAP96072.1; -; Genomic_DNA.
DR RefSeq; XP_002568206.1; XM_002568160.1.
DR AlphaFoldDB; B6HKJ3; -.
DR STRING; 500485.B6HKJ3; -.
DR GeneID; 8310421; -.
DR KEGG; pcs:Pc21g11750; -.
DR VEuPathDB; FungiDB:PCH_Pc21g11750; -.
DR eggNOG; KOG1712; Eukaryota.
DR HOGENOM; CLU_063339_1_0_1; -.
DR OMA; QAYDLEY; -.
DR OrthoDB; 231465at2759; -.
DR BioCyc; PCHR:PC21G11750-MONOMER; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-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 CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR InterPro; IPR005764; Ade_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR NCBIfam; TIGR01090; apt; 1.
DR PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 63..179
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 202 AA; 21634 MW; B37953C5C2C90370 CRC64;
MSSTTPDASK VGLPASDATS AAELASLKVR LRAALRQFPD FPSPGILFED ILPIFADPSL
HEALIRSLEL HVLTNYGQKP DVIVGLEARG FLMGPSLALR LGASFVPVRK QGKLPGPCET
QGYQKEYGQD FFQMQADSIK PGQKVLVIDD IIATGGSAKA GGELIQKMGG ELLGFIFLLE
LEFLHGRDNL PAPVYTLLSG QA
//
