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
//