ID Q9GQ67_DROYA Unreviewed; 560 AA.
AC Q9GQ67;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 Name=Pgm {ECO:0000313|EMBL:AAG42303.1};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:AAG42303.1};
RN [1] {ECO:0000313|EMBL:AAG42303.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BG1013 {ECO:0000313|EMBL:AAG42303.1};
RX PubMed=11102370;
RA Verrelli B.C., Eanes W.F.;
RT "Extensive amino acid polymorphism at the pgm locus is consistent with
RT adaptive protein evolution in Drosophila melanogaster.";
RL Genetics 156:1737-1752(2000).
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; AF290370; AAG42303.1; -; Genomic_DNA.
DR RefSeq; XP_002095770.1; XM_002095734.2.
DR AlphaFoldDB; Q9GQ67; -.
DR GeneID; 6535107; -.
DR OrthoDB; 5476118at2759; -.
DR ChiTaRS; Pgm; fly.
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 CDD; cd03085; PGM1; 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; IPR005843; A-D-PHexomutase_C.
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 Pfam; PF00408; PGM_PMM_IV; 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:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 16..156
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 192..297
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 308..420
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 479..526
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 560 AA; 60854 MW; DCAF560F96EBDD87 CRC64;
MSLTVEIVTT KPYEGQKPGT SGLRKKVKVF TQPNYTENFV QAILEANGAA LVGSTLVVGG
DGRFYCKEAA ELIVRLSAAN GVSKLLVGQN GILSTPAVSS LIRHNKALGG IVLTASHNPG
GPENDFGIKF NCENGGPAPD AFTNLIYKIT TEIKQYKLVR NLQIDITKVG VTLYDIAGKP
FTVEVIDSVA NYVRHMEEIF DFAKLKDFVS GKATGKPLKM RIDAMNGVTG SYVREIFLNR
LGATESSVVH TTPLPDFGGL HPDPNLTYAK DLVDTVAQGD YDIGAAFDGD GDRNMIIGSK
AFFVTPSDSL AVIAHYLEAI PYFQKNGVQG FARSMPTASA VDLVGRKLGK EVFEVPTGWK
YFGNLMDAGR LCLCGEESFG TGSNHIREKD GIWAVLAWIS VMQHTGKGIE DILKQHWSVY
GRNYFTRYDY EECASDPCNE MVATMEKTIT APEFVGKSYS SGGKTYKVKK ADNFSYTDPV
DKSVATKQGL RIVFEDGSRI VVRLSGTGSS GATVRLYIDS YEQENVLGQA SVMLKPLIDI
ALEISQLPKF TGRNAPTVIT
//
