ID W4J2N1_PLAFP Unreviewed; 806 AA.
AC W4J2N1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Hypoxanthine-guanine-xanthine phosphoribosyltransferase {ECO:0000313|EMBL:ETW56538.1};
GN ORFNames=PFUGPA_01328 {ECO:0000313|EMBL:ETW56538.1};
OS Plasmodium falciparum (isolate Palo Alto / Uganda).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW56538.1, ECO:0000313|Proteomes:UP000019103};
RN [1] {ECO:0000313|EMBL:ETW56538.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW56538.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW56538.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW56538.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; KI927303; ETW56538.1; -; Genomic_DNA.
DR AlphaFoldDB; W4J2N1; -.
DR EnsemblProtists; ETW56538; ETW56538; PFUGPA_01328.
DR OMA; HVTKASY; -.
DR Proteomes; UP000019103; Unassembled WGS sequence.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:InterPro.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR CDD; cd05799; PGM2; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005904; Hxn_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR NCBIfam; TIGR01203; HGPRTase; 1.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:ETW56538.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019103};
KW Transferase {ECO:0000313|EMBL:ETW56538.1}.
FT DOMAIN 49..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 222..326
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 337..442
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 625..780
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 806 AA; 92448 MW; 07D6A41F59057E9F CRC64;
MENIKNEQVM KFLELWNIFK KPQYLIDETI EILKKNDEEE LKCLFLKRLN FGTAGLRGKM
GVGFNAMNVV TIMQTTQGLC SYLINTYGLN LCKNRGIIFG FDGRYHSESF AHVAASVCLS
KGFRVYLFAQ TVATPILCYS NLKKNCLCGV MVTASHNPKL DNGYKVYASN GAQIIPPVDK
NISNCILNNL EPWKDAYEYL NENFYLKDTS LVEDIYFEMY DSFMDDLKHE FNFNCYRNSR
TKLAIVYSPM HGIGRKFVQG IMHVVGFNNL LTVPQQALPD SDFSTVSFPN PEEKGALDMS
MELADKVCSP IVVANDPDAD RFACAEKFNN KWKVFSGDEL GIIFAYHLMK QYEKKNIDKS
KHVFLCTVVC SRMLKKLCEK YGYKYDETLT GFKWLINKAI EYNEQNYTIL YCYEEALGHA
LTRHVKDKCG ISALGYWIEI AVYLYENNLT FHQYLETIRE EIGYFVNNNG YYIVLDSNDI
VSIFNEFRSN GLYKTNLGSY KIIHIRDLTT GYDSTTADKK SLIAPTPDSQ NITIHFENTA
ILTIRASGTE PKVKWYAEIS RDTYEQAKKE IDQLIDEVMP IPGAGENAFD PVFVKDDDGY
DLDSFMIPAH YKKYLTKVLV PNGVIKNRIE KLAYDIKKVY NNEEFHILCL LKGSRGFFTA
LLKHLSRIHN YSAVETSKPL FGEHYVRVKS YCNDQSTGTL EIVSEDLSCL KGKHVLIVED
IIDTGKTLVK FCEYLKKFEI KTVAIACLFI KRTPLWNGFK ADFVGFSIPD HFVVGYSLDY
NEIFRDLDHC CLVNDEGKKK YKATSL
//
