ID K2NUY3_TRYCR Unreviewed; 613 AA.
AC K2NUY3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 27.
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};
DE Flags: Fragment;
GN ORFNames=MOQ_000991 {ECO:0000313|EMBL:EKF38801.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF38801.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF38801.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF38801.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
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:EKF38801.1}.
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DR EMBL; AHKC01004996; EKF38801.1; -; Genomic_DNA.
DR AlphaFoldDB; K2NUY3; -.
DR EnsemblProtists; EKF38801; EKF38801; MOQ_000991.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000007350; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..613
FT /note="phosphoglucomutase (alpha-D-glucose-1,6-
FT bisphosphate-dependent)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003862599"
FT DOMAIN 41..185
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 342..469
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKF38801.1"
SQ SEQUENCE 613 AA; 67312 MW; 38CB9B70559057D3 CRC64;
FFFFFFFFFL VHSVNLGASQ CVVSQIMLTV KKVPTRPFID QKPGTSGLRK KVRVFQQENY
LANFVQSTFN AIGKQGMIPD TLVLGGDGRY FLSEAIQIII KLAAANGVSN VWVGKDGLLS
TPAVSNIIRQ RRDGDVKAKG AFILTASHNP GGPEEDFGIK YNTENGGPAS EKITSAIYEE
TLKIDHFLTC PNIGTVNVSE MGDHVFERFR VSVIHSTEDY VQSMKKIFDF QSIQNLLNRP
DFKIRLDGLS GIGGPYMKDI FVSSLGVSEG ALCGATPLPD FGKQHPDPNL TYAKELVRAM
GLDSTGTPVA DFVGEIPNFA AAFDGDADRN MILGKRFFVT PSDSLAILAA NASVVPFFAQ
QGGLKAVARS MPTSGAVDRV AEMHHLKIFE VPTGWKFFGN LMDSREVFGG EDYNPLICGE
ESFGTGSNHI REKDGLWAAL FWLSVIASKN VDPTKPLVGV KEIVEDHWTR YGRNYYCRYD
YENVAEDSAK AVMETVQGHR PQDIPSLQGK RCVKVDNFEY HDPVDGLVSK NQGIRVIFED
GSRFVIRLSG TGSSDATIRL YLELYMEPNA VARHIRDGTL PTPQSALANL IAIALNVSQI
SGLTGRDAPT VIT
//
