ID A0A179GN60_PURLI Unreviewed; 230 AA.
AC A0A179GN60;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN ORFNames=VFPFJ_09833 {ECO:0000313|EMBL:OAQ79347.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ79347.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ79347.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ79347.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAQ79347.1}.
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DR EMBL; LSBI01000010; OAQ79347.1; -; Genomic_DNA.
DR RefSeq; XP_018174364.1; XM_018326902.1.
DR AlphaFoldDB; A0A179GN60; -.
DR STRING; 33203.A0A179GN60; -.
DR GeneID; 28891951; -.
DR KEGG; plj:VFPFJ_09833; -.
DR OMA; QAYDLEY; -.
DR OrthoDB; 231465at2759; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000078340; Unassembled WGS sequence.
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 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 ECO:0000313|EMBL:OAQ79347.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726};
KW Reference proteome {ECO:0000313|Proteomes:UP000078340};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAQ79347.1}.
FT DOMAIN 85..177
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 230 AA; 24102 MW; 9F8B9F7CF1DAF87A CRC64;
MTALPPDHAA PESSSSSTLP ATTATAAQDA SGRQPSSAAS AAAELASAKI SLRKSLRQFP
DFPIPGIDFV DIMPLFANPD AHATLVSALE LQIAQTFAQA KPDVIVGLDA RGFLFGPGLA
LRLGVPFAAV RKQGKLPGPC VTAEYVKEYG KDLFQMQEDA IREGQKVLVV DDIIATGMFR
VLSGSAKAAA DLVAQLKGQV MGYLFILEIP GLNGRDKLGE APTTILLEDA
//
