ID A0A0R1HK56_9LACO Unreviewed; 179 AA.
AC A0A0R1HK56;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN ORFNames=FC96_GL000803 {ECO:0000313|EMBL:KRK47037.1};
OS Secundilactobacillus kimchicus JCM 15530.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK47037.1, ECO:0000313|Proteomes:UP000050911};
RN [1] {ECO:0000313|EMBL:KRK47037.1, ECO:0000313|Proteomes:UP000050911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK47037.1,
RC ECO:0000313|Proteomes:UP000050911};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRK47037.1}.
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DR EMBL; AZCX01000013; KRK47037.1; -; Genomic_DNA.
DR RefSeq; WP_056943128.1; NZ_AZCX01000013.1.
DR AlphaFoldDB; A0A0R1HK56; -.
DR STRING; 1302272.FC96_GL000803; -.
DR PATRIC; fig|1302272.5.peg.803; -.
DR OrthoDB; 9802824at2; -.
DR UniPathway; UPA00591; UER00648.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000050911; 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:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
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|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU364099};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364099};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364099};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364099};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW ECO:0000256|RuleBase:RU364099};
KW Reference proteome {ECO:0000313|Proteomes:UP000050911};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT DOMAIN 12..160
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 179 AA; 20070 MW; 064A007E094A0636 CRC64;
MNNDIERVLF SQEDIQEACR RLGAQISRDY EGKKPVVVGV LKGAILFMVD LIKEMDIMTE
VDFLDVSSYH GGVASTGSIT LNREIETDIS GRHVIIVEDI IDTGLTLQYM LNYLNAHHVA
SAKVCTLLDK PEGRKVTAKA DYVGFNVPNE FVVGYGLDYQ EFYRNLPYVG VLKPDVYSE
//
