ID A0A090L9K9_STRRB Unreviewed; 169 AA.
AC A0A090L9K9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN ORFNames=SRAE_2000110500 {ECO:0000313|EMBL:CEF66437.1,
GN ECO:0000313|WBParaSite:SRAE_2000110500.1,
GN ECO:0000313|WormBase:SRAE_2000110500};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF66437.1};
RN [1] {ECO:0000313|EMBL:CEF66437.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000110500.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF66437.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000110500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; LN609529; CEF66437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L9K9; -.
DR STRING; 34506.A0A090L9K9; -.
DR EnsemblMetazoa; SRAE_2000110500.1; SRAE_2000110500.1; WBGene00261307.
DR WBParaSite; SRAE_2000110500.1; SRAE_2000110500.1; WBGene00261307.
DR WormBase; SRAE_2000110500; SRP02798; WBGene00261307; -.
DR OMA; ITHFVYH; -.
DR OrthoDB; 231465at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:CEF66437.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEF66437.1}.
FT DOMAIN 45..148
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 169 AA; 18922 MW; EDC5FA530792D66E CRC64;
MENNSKAFDN VKERIKNRLV DYPDFPKKGI LFRDIMPLFK DPVLINDLAL SIANYFKNSQ
INSIAACEAR GFLFGVIVSI HMNVPFVAIR KKEYGEDIFE VQKNSFKSGD RVLILDDLLA
TGGSMSAAID VVKKAGANPV NAFCLVELTE LKGREKLPES TIFEAMIQF
//
