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Database: UniProt
Entry: C6JM37_FUSVA
LinkDB: C6JM37_FUSVA
Original site: C6JM37_FUSVA 
ID   C6JM37_FUSVA            Unreviewed;       188 AA.
AC   C6JM37;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01184};
DE            Short=XPRTase {ECO:0000256|HAMAP-Rule:MF_01184};
DE            EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01184};
GN   Name=xpt {ECO:0000256|HAMAP-Rule:MF_01184,
GN   ECO:0000313|EMBL:EES63882.1};
GN   ORFNames=FVAG_02642 {ECO:0000313|EMBL:EES63882.1};
OS   Fusobacterium varium ATCC 27725.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=469618 {ECO:0000313|EMBL:EES63882.1, ECO:0000313|Proteomes:UP000004505};
RN   [1] {ECO:0000313|EMBL:EES63882.1, ECO:0000313|Proteomes:UP000004505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES63882.1,
RC   ECO:0000313|Proteomes:UP000004505};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium varium ATCC 27725.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts the preformed base xanthine, a product of nucleic
CC       acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be
CC       reused for RNA or DNA synthesis. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01184};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC       from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Xpt subfamily. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EES63882.1}.
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DR   EMBL; ACIE02000021; EES63882.1; -; Genomic_DNA.
DR   RefSeq; WP_005950541.1; NZ_GL987999.1.
DR   AlphaFoldDB; C6JM37; -.
DR   STRING; 469618.FVAG_02642; -.
DR   GeneID; 77469018; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_099015_0_0_0; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000004505; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0046110; P:xanthine metabolic process; IEA:InterPro.
DR   GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01184; XPRTase; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR010079; Xanthine_PRibTrfase.
DR   NCBIfam; TIGR01744; XPRTase; 1.
DR   PANTHER; PTHR43864; HYPOXANTHINE/GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43864:SF1; HYPOXANTHINE_GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01184};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01184,
KW   ECO:0000313|EMBL:EES63882.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_01184}; Reference proteome {ECO:0000313|Proteomes:UP000004505};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01184}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..162
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         20
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT   BINDING         27
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT   BINDING         127..131
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT   BINDING         155
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
SQ   SEQUENCE   188 AA;  20511 MW;  0D6FDC18A44F069C CRC64;
     MKLLKEYIEK NGKAIGTNIL KVDSFLNHQI DPNLMMAMGE EFKRRFKDQG VNKILTIEAS
     GIAIGLAAAY AFNVPLVFAK KKIPSTMGDF YTTNVFSFTK NKDYTICVAK EFLTPNDKVL
     IVDDFLAMGN AVLGLKTLVE SAGAIVIGAG IAVEKGFQQG EKLLTDNGIK VEALAVVDSL
     ENGIIKFR
//
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