APT_CHLCH
ID APT_CHLCH Reviewed; 177 AA.
AC Q3AT37;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004};
DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004};
GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=Cag_0565;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) 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:0000255|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:0000255|HAMAP-Rule:MF_00004};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB27838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000108; ABB27838.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041466430.1; NC_007514.1.
DR AlphaFoldDB; Q3AT37; -.
DR SMR; Q3AT37; -.
DR STRING; 340177.Cag_0565; -.
DR EnsemblBacteria; ABB27838; ABB27838; Cag_0565.
DR KEGG; cch:Cag_0565; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_10; -.
DR OrthoDB; 1532478at2; -.
DR UniPathway; UPA00588; UER00646.
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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01090; apt; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..177
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000321354"
SQ SEQUENCE 177 AA; 19265 MW; 4959AEA0818E207E CRC64;
MPIKSRIRSI PDYPKKGIMF RDITTLIKDP VGFRLVIDHL TQHYLEAGMD FDVIVGIEAR
GFIIGGALSY TLGKGFVPVR KPGKLPADVV SQEYELEYGS DKIEIHTDAL VEGQRVLLVD
DLLATGGTAL AAAALVEKVG GIVAEMAFIV NLPDVGGERK LLEKGYNVYS LTDFEGD