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Database: UniProt
Entry: F6HDE0_VITVI
LinkDB: F6HDE0_VITVI
Original site: F6HDE0_VITVI 
ID   F6HDE0_VITVI            Unreviewed;       107 AA.
AC   F6HDE0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE            EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN   ORFNames=VIT_00s1847g00010 {ECO:0000313|EMBL:CCB50235.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391}.
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DR   EMBL; FN595704; CCB50235.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HDE0; -.
DR   STRING; 29760.F6HDE0; -.
DR   PaxDb; 29760-VIT_00s1847g00010-t01; -.
DR   eggNOG; KOG1712; Eukaryota.
DR   HOGENOM; CLU_063339_5_2_1; -.
DR   InParanoid; F6HDE0; -.
DR   Proteomes; UP000009183; Unassembled WGS sequence, unordered.
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; PTHR11776; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11776:SF7; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..107
FT                   /note="adenine phosphoribosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003340833"
FT   DOMAIN          32..92
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   107 AA;  11763 MW;  CC8E2237D1BF7AA6 CRC64;
     MANLLLHFLA FNLTSRAIMT GEVISEEYIL EYGRDCLEMH VGAVEPGDRA LVVDDLIATG
     GTLCAAMNLL ERVGAEVVEC ACVIELPDLK GRDRLNGKPL YILVEYH
//
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