ID A0A397GQS3_9EURO Unreviewed; 237 AA.
AC A0A397GQS3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN ORFNames=CDV56_100050 {ECO:0000313|EMBL:RHZ53362.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ53362.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ53362.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ53362.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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:RHZ53362.1}.
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DR EMBL; NKHU02000124; RHZ53362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397GQS3; -.
DR STRING; 41047.A0A397GQS3; -.
DR VEuPathDB; FungiDB:CDV56_100050; -.
DR OrthoDB; 231465at2759; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000215305; 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; -; 2.
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; 2.
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:UP000215305};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 82..166
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 25624 MW; D4E5F76E6F285D6F CRC64;
MSQSTPSQST QTPDAAAAQV AGHPSSHPSR TTELSSLKVR LRAALRQFPD FPSPGILFED
ILPIFADPTL HEALLRCLEL HILETHSNQK PDVIVGLEAR GFLFGPSLAL RLGASFVPVR
KKGKLPGPCE TQGYEKEYGQ DFFQMQADAI KPGQKVIVVD DIIATGEFVL SQEIPSSSSF
VDLVTGGSAY AAGELIKKMG GELMGFIFIL ELEFLKGRDK LPAPVYTLLS GQEAKSL
//
