ID Q4DLI9_TRYCC Unreviewed; 600 AA.
AC Q4DLI9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Tc00.1047053508637.90 {ECO:0000313|EMBL:EAN93386.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN93386.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN93386.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN93386.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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}.
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:EAN93386.1}.
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DR EMBL; AAHK01000352; EAN93386.1; -; Genomic_DNA.
DR RefSeq; XP_815237.1; XM_810144.1.
DR AlphaFoldDB; Q4DLI9; -.
DR SMR; Q4DLI9; -.
DR STRING; 353153.Q4DLI9; -.
DR PaxDb; 353153-Q4DLI9; -.
DR EnsemblProtists; EAN93386; EAN93386; Tc00.1047053508637.90.
DR GeneID; 3546934; -.
DR KEGG; tcr:508637.90; -.
DR eggNOG; KOG0625; Eukaryota.
DR InParanoid; Q4DLI9; -.
DR OMA; WIQDRAN; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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; 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; 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 Isomerase {ECO:0000313|EMBL:EAN93386.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296}.
FT DOMAIN 28..172
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 331..442
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 600 AA; 65900 MW; AFC2F390683E0C37 CRC64;
MNLGETQCVV FQIMLAVKKV PTRPFIDQQP GTSGLRKKVR VFQQENYLAN FIQSTFNAIG
KQGMIPDTLV LGGDGRYFLS EAIQIIIKLA AANGVSNVWV GKDGLLSTPA VSNIIRQRRD
GDVTAKGAFI LTASHNPGGP EEDFGIKYNT ENGGPAAEKI TSAIYEETLK IDHFLTCPNI
GTVNVSEMGD HLFERFRVSV IHSTEDYVQS MKKIFDFQSI RNLLNRTDFT IRLDGLSGIG
GPYMKDIFVS ALGVPESALC GATPLPDFGK QHPDPNLTYA KELVRTMGLD STGRPVADFV
GEVPNFAAAF DGDADRNMIL GERFFVTPSD SLAILSANAN VVPFFAQQGG IKAVARSMPT
SGAVDRVAEM HHLKIFEVPT GWKFFGNLMD SRELFGGEDY NPLICGEESF GTGSNHIREK
DGVWAALFWL SVIASKNVDP SKPLVGVKDI VEDHWTRYGR NYYCRYDYEN VAEDSAKAVM
ETVQRQRPQD IPSLQGKRCV KVDNFEYHDP VDGLVSKNQG IRVIFEDGSR FVIRLSGTGS
SGATIRLYLE HYMEPNAVAR HIRDGTLPTP QSALANLIAV ALNVSQISEL TGRDAPTVIT
//
