ID F2NW87_TRES6 Unreviewed; 192 AA.
AC F2NW87;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Tresu_2139 {ECO:0000313|EMBL:AEB15008.1};
OS Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=869209 {ECO:0000313|EMBL:AEB15008.1, ECO:0000313|Proteomes:UP000006852};
RN [1] {ECO:0000313|EMBL:AEB15008.1, ECO:0000313|Proteomes:UP000006852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33096 / DSM 2489 / 6091
RC {ECO:0000313|Proteomes:UP000006852};
RX PubMed=21886863;
RA Han C., Gronow S., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Zeytun A., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N.,
RA Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Treponema succinifaciens type strain (6091).";
RL Stand. Genomic Sci. 4:361-370(2011).
RN [2] {ECO:0000313|Proteomes:UP000006852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33096 / DSM 2489 / 6091
RC {ECO:0000313|Proteomes:UP000006852};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Treponema succinifaciens DSM 2489.";
RL Submitted (APR-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}.
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DR EMBL; CP002631; AEB15008.1; -; Genomic_DNA.
DR RefSeq; WP_013702261.1; NC_015385.1.
DR AlphaFoldDB; F2NW87; -.
DR STRING; 869209.Tresu_2139; -.
DR KEGG; tsu:Tresu_2139; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_099015_0_0_12; -.
DR OrthoDB; 9783570at2; -.
DR UniPathway; UPA00602; UER00658.
DR Proteomes; UP000006852; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:AEB15008.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_01184}; Reference proteome {ECO:0000313|Proteomes:UP000006852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01184}.
FT DOMAIN 23..158
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 129..133
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 157
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
SQ SEQUENCE 192 AA; 20897 MW; B3B292F1F343A14C CRC64;
MKLLEDRIKK DGIVLPGNIL KVNSFLNHQI DVDLLDKLAE DFKKSFDGVD ITKIVTIEAS
GIAVACSVAR AFGNVPVLFA KKHKSAALSD DVYYSTVWSH TNSCNYNIVI SREYLSSDDK
ILLVDDFLAN GNAMNGLIEI AENAGAKVQG ICVAIEKAFQ SGGDALREKG IHVESGAIIE
KMSYNGDIIF RS
//
