ID W6LBK3_9TRYP Unreviewed; 591 AA.
AC W6LBK3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=GSHART1_T00002451001 {ECO:0000313|EMBL:CCW71795.1};
OS Phytomonas sp. Hart1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW71795.1, ECO:0000313|Proteomes:UP000053358};
RN [1] {ECO:0000313|EMBL:CCW71795.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW71795.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW71795.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW71795.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; HF955215; CCW71795.1; -; Genomic_DNA.
DR AlphaFoldDB; W6LBK3; -.
DR EnsemblProtists; CCW71795; CCW71795; GSHART1_T00002451001.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000053358; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; 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; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000053358}.
FT DOMAIN 16..159
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 192..308
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 317..425
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 591 AA; 64857 MW; 7C05BDEF54E6A2F4 CRC64;
MALEGMEFTT KSYLDQKPGT SGLRKKVSVF EQENYIANFV QSTFNALRLL NSFPEVLVVG
GDGRYYMKEA IQIILRVAMA NGVQSVWVGH KGLLSTPAVS TVIRRRSGGF KAQGAFILTA
SHNPGGPDAD FGIKYNTANG GPAPEKVTEV IYNETLKIST LYLNSSLPEV DLTRIGVQTY
DHFTVEVISS VEDYISYMKE IFDFDAIGSF LSRPDFTIHL DCLHGASGPY VQEIFHTCLG
VPLASLHHTT PLSDFGGYHP DPNLTYAHNL VQVMGLLPNG SIDRSRAGEQ VPSFGAAFDG
DADRNMILGS RFFVNPSDSL AILVANAEVI PFFRKAGGLS SVARSMPTSC AVDRVAQERN
LRCFEVPTGW KFFGNLMDSK TVFGGEDYNP FICGEESFGT GSNHIREKDG VWTCLFWLSL
LASKNDPGVN PSRSLVGVQS IVEQHWALYG LNYYTRYDYE NVSVDSANTV MENILSKLPE
EIPCLDGKRC CIVDSFEYCD PIDGSITSKQ GVRVVFEDNS RFVLRLSSTG TSGATIRLYL
EKYVGPAFVT DNLRKGTLPP SSEGLRELIQ ISLDVSKIPE ATGRDAPTVI T
//
