PGMC2_MAIZE
ID PGMC2_MAIZE Reviewed; 583 AA.
AC P93805;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phosphoglucomutase, cytoplasmic 2;
DE Short=PGM 2;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase 2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73;
RX PubMed=9662542; DOI=10.1104/pp.117.3.997;
RA Manjunath S., Lee C.-H.K., VanWinkle P., Bailey-Serres J.;
RT "Molecular and biochemical characterization of cytosolic phosphoglucomutase
RT in maize: expression during development and in response to oxygen
RT deprivation.";
RL Plant Physiol. 117:997-1006(1998).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; U89342; AAC50049.1; -; mRNA.
DR PIR; T04327; T04327.
DR RefSeq; NP_001105405.1; NM_001111935.1.
DR AlphaFoldDB; P93805; -.
DR SMR; P93805; -.
DR STRING; 4577.GRMZM2G023289_P01; -.
DR iPTMnet; P93805; -.
DR PaxDb; P93805; -.
DR PRIDE; P93805; -.
DR GeneID; 542358; -.
DR KEGG; zma:542358; -.
DR MaizeGDB; 12544; -.
DR eggNOG; KOG0625; Eukaryota.
DR OrthoDB; 555015at2759; -.
DR BRENDA; 5.4.2.2; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P93805; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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; PTHR22573; 2.
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; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..583
FT /note="Phosphoglucomutase, cytoplasmic 2"
FT /id="PRO_0000147802"
FT ACT_SITE 124
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 124..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 304..305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 387..389
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 583 AA; 63041 MW; D18F4FFC17A97865 CRC64;
MGLFTVTKKA TTPFEGQKPG TSGLRKKVTV FQQPHYLQNF VQSTFNALPA DQVKGATIVV
SGDGRYFSKD AVQIITKMAA ANGVRRVWVG QNSLMSTPAV SAVIRERIGA DGSKATGAFI
LTASHNPGGP TEDFGIKYNM GNGGPAPESV TDKIFSNTTT ISEYLISEDL PDVDISVVGV
TSFSGPEGPF DVDVFDSSVN YIKLMKTIFD FEAIKKLLTS PKFTFCYDAL HGVAGAYAKH
IFVEELGADE SSLLNCVPKE DFGGGHPDPN LTYAKELVER MGLGKSSSNV EPPEFGAAAD
GDADRNMILG KRFFVTPSDS VAIIAANAVQ SIPYFASGLK GVARSMPTSA ALDVVAKNLN
LKFFEVPTGW KFFGNLMDAG MCSICGEESF GTGSDHIREK DGIWAVLAWL SIIAFKNKDN
LGGDKLVTVE DIVRQHWATY GRHYYTRYDY ENVDAGAAKE LMANLVSMQS SLSDVNKLIK
EIRSDVSEVV AADEFEYKDP VDGSVSKHQG IRYLFGDGSR LVFRLSGTGS VGATIRVYIE
QYEKDSSKTG RDSQEALAPL VDVALKLSKM QEYTGRSAPT VIT
