ID   A0A177PHS5_9RHIZ        Unreviewed;       161 AA.
AC   A0A177PHS5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-OCT-2016, entry version 2.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903, ECO:0000256|SAAS:SAAS00010603};
DE            EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01903, ECO:0000256|SAAS:SAAS00010679};
DE   AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903};
GN   Name=gpt {ECO:0000256|HAMAP-Rule:MF_01903};
GN   ORFNames=A1351_01280 {ECO:0000313|EMBL:OAI29721.1};
OS   Methylosinus sp. R-45379.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylocystaceae; Methylosinus.
OX   NCBI_TaxID=980563 {ECO:0000313|EMBL:OAI29721.1, ECO:0000313|Proteomes:UP000078138};
RN   [1] {ECO:0000313|EMBL:OAI29721.1, ECO:0000313|Proteomes:UP000078138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-45379 {ECO:0000313|EMBL:OAI29721.1,
RC   ECO:0000313|Proteomes:UP000078138};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent
CC       hypoxanthine. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00010659}.
CC   -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose
CC       1-diphosphate + xanthine. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00010674}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01903};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01903};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00010664}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01903,
CC       ECO:0000256|SAAS:SAAS00010651}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01903}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01903}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. XGPT subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01903, ECO:0000256|SAAS:SAAS00538977}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAI29721.1}.
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DR   EMBL; LUUM01000223; OAI29721.1; -; Genomic_DNA.
DR   RefSeq; WP_024878890.1; NZ_LUUM01000223.1.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000078138; Unassembled WGS sequence.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01903; XGPRT; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR023747; Xanthine_Guanine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421185};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078138};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421211, ECO:0000313|EMBL:OAI29721.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421217};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421179};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421207};
KW   Purine salvage {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421168};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01903,
KW   ECO:0000256|SAAS:SAAS00421201, ECO:0000313|EMBL:OAI29721.1}.
FT   REGION       38     39       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01903}.
FT   METAL        96     96       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01903}.
FT   BINDING      99     99       Xanthine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01903}.
FT   BINDING     142    142       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01903}.
SQ   SEQUENCE   161 AA;  17508 MW;  4F4857B4CE71C1FB CRC64;
     MEDKAFPVSW DAFHRDARAL AWRLSAVGGF SAIVAVTRGG LVPAGVVARE LGIRVIDTIG
     VASYQEETQR GEVRVLKPLS ETILTLPSEE VLIVDDLVDT GATAKVVRAL LPNAHFATVY
     AKPQGRPLVD TFVTEVSQDT WIFFPWDTGL SFQAPIARES S
//