ID A0A090ITZ9_9GAMM Unreviewed; 181 AA.
AC A0A090ITZ9;
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, ECO:0000256|HAMAP-Rule:MF_00004};
DE Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
GN Name=apt {ECO:0000256|HAMAP-Rule:MF_00004,
GN ECO:0000313|EMBL:CED71870.1};
GN ORFNames=AWOD_I_1805 {ECO:0000313|EMBL:CED71870.1};
OS Aliivibrio wodanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=80852 {ECO:0000313|EMBL:CED71870.1, ECO:0000313|Proteomes:UP000032427};
RN [1] {ECO:0000313|Proteomes:UP000032427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06/09/139 {ECO:0000313|Proteomes:UP000032427};
RA Hjerde E.;
RL Submitted (SEP-2014) 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|HAMAP-Rule:MF_00004}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00004};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659,
CC ECO:0000256|HAMAP-Rule:MF_00004}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00004}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|HAMAP-
CC Rule:MF_00004}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN554846; CED71870.1; -; Genomic_DNA.
DR RefSeq; WP_045102471.1; NZ_LN554846.1.
DR AlphaFoldDB; A0A090ITZ9; -.
DR STRING; 80852.AWOD_I_1805; -.
DR GeneID; 28541380; -.
DR KEGG; awd:AWOD_I_1805; -.
DR PATRIC; fig|80852.17.peg.1864; -.
DR HOGENOM; CLU_063339_3_0_6; -.
DR OrthoDB; 9803963at2; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000032427; Chromosome 1 complete sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-UniRule.
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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00004};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004,
KW ECO:0000313|EMBL:CED71870.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_00004};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000313|EMBL:CED71870.1}.
FT DOMAIN 30..150
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 181 AA; 19648 MW; 15CF03F4A5B5F585 CRC64;
MSTETLELIK NSIKSIPDYP KVGIMFRDVT SLMEEPKAYQ ATIQLLVEKY KDGGFTKIIG
TEARGFLFGA PLALELGVGF IPVRKPGKLP RPTIAQTYDL EYGTDTLEIH TDAIVEGDKV
LVVDDLLATG GTIEATVKLI RQLGGNVEHA AFVINLPEIG GQTRLEGLGL NVYSICEFAG
H
//