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Database: UniProt
Entry: A0A0B4S1C4_9FIRM
LinkDB: A0A0B4S1C4_9FIRM
Original site: A0A0B4S1C4_9FIRM 
ID   A0A0B4S1C4_9FIRM        Unreviewed;       173 AA.
AC   A0A0B4S1C4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   Name=hpt {ECO:0000313|EMBL:AXU10461.1};
GN   ORFNames=DYJ31_03970 {ECO:0000313|EMBL:AXU10461.1}, HXM94_02510
GN   {ECO:0000313|EMBL:MBF1306653.1}, NND69_00460
GN   {ECO:0000313|EMBL:MCZ7406842.1}, NW74_04180
GN   {ECO:0000313|EMBL:AIZ36583.1};
OS   Parvimonas micra.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Parvimonas.
OX   NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ36583.1, ECO:0000313|Proteomes:UP000031386};
RN   [1] {ECO:0000313|EMBL:AIZ36583.1, ECO:0000313|Proteomes:UP000031386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCOM 1535 {ECO:0000313|EMBL:AIZ36583.1}, and KCOM 1535 / ChDC
RC   B708 {ECO:0000313|Proteomes:UP000031386};
RA   Kook J.-K., Park S.-N., Lim Y.K., Roh H.;
RT   "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC B708).";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AXU10461.1, ECO:0000313|Proteomes:UP000258329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCOM 1037 {ECO:0000313|EMBL:AXU10461.1,
RC   ECO:0000313|Proteomes:UP000258329};
RA   Kook J.-K., Park S.-N., Lim Y.K.;
RT   "Genome sequencing of Parvimonas micra KCOM 1037.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MBF1306653.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCVI_23_bin.11 {ECO:0000313|EMBL:MBF1306653.1};
RA   Baker J.L., Morton J.T., Dinis M., Alvarez R., Tran N.C., Knight R.,
RA   Edlund A.;
RT   "Deep metagenomics examines the oral microbiome during advanced dental
RT   caries in children, revealing novel taxa and co-occurrences with host
RT   molecules.";
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:MCZ7406842.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PM79KC-AC-4 {ECO:0000313|EMBL:MCZ7406842.1};
RA   Conde-Perez K., Buetas E., Aja-Macaya P., Martin-De Arribas E.,
RA   Iglesias-Corras I., Trigo-Tasende N., Nasser-Ali M., Estevez L.S.,
RA   Rumbo-Feal S., Otero-Alen B., Noguera J.F., Concha A., Pardinas-Lopez S.,
RA   Carda-Dieguez M., Gomez-Randulfe I., Martinez-Lago N., Ladra S.,
RA   Aparicio L.A., Bou G., Mira A., Vallejo J.A., Poza M.;
RT   "Parvimonas micra travels from the subgingival sulcus of the human oral
RT   cavity to the colorectal adenocarcinoma.";
RL   Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of
CC       the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-
CC       diphosphate (PRPP) to the N9 position of the 6-oxopurines hypoxanthine
CC       and guanine to form the corresponding ribonucleotides IMP (inosine 5'-
CC       monophosphate) and GMP (guanosine 5'-monophosphate), with the release
CC       of PPi. {ECO:0000256|ARBA:ARBA00002049}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000210};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC         Evidence={ECO:0000256|ARBA:ARBA00000210};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001442};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC         Evidence={ECO:0000256|ARBA:ARBA00001442};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU364099};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC       from guanine: step 1/1. {ECO:0000256|ARBA:ARBA00004676}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000256|ARBA:ARBA00004669,
CC       ECO:0000256|RuleBase:RU364099}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU364099}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|RuleBase:RU364099}.
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DR   EMBL; CP009761; AIZ36583.1; -; Genomic_DNA.
DR   EMBL; CP031971; AXU10461.1; -; Genomic_DNA.
DR   EMBL; JABZRE010000005; MBF1306653.1; -; Genomic_DNA.
DR   EMBL; JANDZV010000001; MCZ7406842.1; -; Genomic_DNA.
DR   RefSeq; WP_004833313.1; NZ_RKIS01000001.1.
DR   STRING; 33033.NW74_04180; -.
DR   GeneID; 71955184; -.
DR   KEGG; pmic:NW74_04180; -.
DR   OrthoDB; 9802824at2; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000031386; Chromosome.
DR   Proteomes; UP000258329; Chromosome.
DR   Proteomes; UP000758611; Unassembled WGS sequence.
DR   Proteomes; UP001141458; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032264; P:IMP 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   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   NCBIfam; TIGR01203; HGPRTase; 1.
DR   PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:AIZ36583.1}; Magnesium {ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364099};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW   ECO:0000256|RuleBase:RU364099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031386};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT   DOMAIN          12..158
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   173 AA;  19936 MW;  8FB9AD98CBC68A90 CRC64;
     MNKREVTRFT REEIANKVKE LGKQISKDYT GKELVAIGLL RGSFVFLADL VREIDNPIVV
     DFITTSSYEH SEISTGTVNI LSDLRENIEG KDVLIVDDIM DSGNTLKNIR EYILTKNPNS
     VKTCVMLDKP CRREVDIVPD YFGFEIEDWF IVGYGLNYGN KYRNIPYIFS YED
//
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