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Database: UniProt
Entry: W4ISD6_PLAFP
LinkDB: W4ISD6_PLAFP
Original site: W4ISD6_PLAFP 
ID   W4ISD6_PLAFP            Unreviewed;       927 AA.
AC   W4ISD6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Phosphoacetylglucosamine mutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PFUGPA_05242 {ECO:0000313|EMBL:ETW52935.1};
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:ETW52935.1, ECO:0000313|Proteomes:UP000019103};
RN   [1] {ECO:0000313|EMBL:ETW52935.1, ECO:0000313|Proteomes:UP000019103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW52935.1,
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:ETW52935.1, ECO:0000313|Proteomes:UP000019103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW52935.1,
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; KI927387; ETW52935.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4ISD6; -.
DR   EnsemblProtists; ETW52935; ETW52935; PFUGPA_05242.
DR   OMA; CTKTGIK; -.
DR   Proteomes; UP000019103; Unassembled WGS sequence.
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   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 1.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR049023; AMG1_II.
DR   InterPro; IPR049022; AMG1_III.
DR   PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   Pfam; PF21405; AMG1_II; 1.
DR   Pfam; PF21404; AMG1_III; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019103}.
FT   DOMAIN          204..245
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          465..579
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21405"
FT   DOMAIN          666..819
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21404"
FT   DOMAIN          875..915
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          88..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   927 AA;  110113 MW;  ECFD8192860DB889 CRC64;
     MKDFKESWFY KKIKPCIKKY MPKYTNEGHI IFQNPYEFSY GNCGYREKYN LSSCDLLNAI
     NKCGIFVGLL FIKYNYDIIF NQKEKRNDFT TTKGNNNNYE NKDENNEKKN EKKNEKKNKN
     KNEKKNKNKN ENNEKKNENK NKNKNENNEN TNENNKNNKN NKNNKNNSNS NNNNNYYYYN
     HYNMCEKIHK DLVYNYNEYI KLKNVGIIIT ASHNPHDENG IKIIGVDGKY INKTYENYLI
     ELVNNHLRYI KKNVNCTCDD IINNTIELIV DIFKKEINLD ISDDIIYENI SILDDIIYNY
     NIHNKIKTNI CIGFDTRNSN IHLNNIIIES LNCLNIYKCI NNITYITTPC MHFLIYFLNY
     INENDEKIDK QIIQQEEYTI HKKSNDLSYL KNFHIQNNKS VYYLYYSKYD QYLTNEVLTT
     NGTPLQQPFN ISIQQHIEKE KEKKNSHENN NFIYTHMEHI YAYNSDQIYF DYFIYSFEML
     YNYITKLFHN NHMMMDMENI YLDCSNGIAS LKIDKFYPIF QILKKNICKF NCIEGEHSIL
     NYECGAEYVY RKQQPPKNVP PIIKHNTKFC TFDGDADRIL YFFFPQKGEE IKKKIFNDGN
     EKNKNNHTDI NINCNMIYNM IYNNNNNINC KDNNFHSTIS DFSKEQMDYY DANIDTCKNN
     QIAILDGPKI ICLFFLCIIK MLSHIKLEEL KEEIPIIDLN IIHTAYTNSA FLNYINYIKN
     NIIVSINIFK YININILCTK TGMKYLDHLA QKACIGIFFE PNGHGTIYVD INKLQKWSLS
     LHINYDLSFI ALQKYLLFFN QTVGDAFLDF IAIELSLSIL NITINEWNNF YTPFPSMYIN
     INCPKHILPK IIPHPKHEQY LIEPITLQTH INQIVNSVDQ QHGRCFVRPS GTENLLRIYA
     EAQTEQKMKD ILDKARTCVL HYIEHIL
//
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