ID PGMC1_MAIZE Reviewed; 583 AA.
AC P93804;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Phosphoglucomutase, cytoplasmic 1 {ECO:0000303|PubMed:9662542};
DE Short=PGM 1 {ECO:0000303|PubMed:9662542};
DE EC=5.4.2.2 {ECO:0000269|PubMed:9662542};
DE AltName: Full=Glucose phosphomutase 1 {ECO:0000303|PubMed:9662542};
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], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, REPRESSION BY HYPOXIA, AND
RP AUTOPHOSPHORYLATION.
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|UniProtKB:P00949}.
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:0000269|PubMed:9662542};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00949};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:9662542}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and coleoptiles, and, to
CC a lower extent, in leaves, pollen and developing seeds.
CC {ECO:0000269|PubMed:9662542}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryo development, with a
CC slight decrease during endosperm development, and fades out during
CC aleurone development. {ECO:0000269|PubMed:9662542}.
CC -!- INDUCTION: Repressed in O(2) deprivated (hypoxia/anoxia) conditions.
CC {ECO:0000269|PubMed:9662542}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:9662542}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; U89341; AAC50048.1; -; mRNA.
DR PIR; T04326; T04326.
DR RefSeq; NP_001105703.1; NM_001112233.1.
DR AlphaFoldDB; P93804; -.
DR SMR; P93804; -.
DR STRING; 4577.P93804; -.
DR iPTMnet; P93804; -.
DR PaxDb; 4577-GRMZM2G109383_P01; -.
DR GeneID; 542721; -.
DR KEGG; zma:542721; -.
DR MaizeGDB; 12543; -.
DR eggNOG; KOG0625; Eukaryota.
DR InParanoid; P93804; -.
DR OrthoDB; 5476118at2759; -.
DR BRENDA; 5.4.2.2; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P93804; 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; IDA:CACAO.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..583
FT /note="Phosphoglucomutase, cytoplasmic 1"
FT /id="PRO_0000147801"
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; 63097 MW; 4C19D15AEF4A6D80 CRC64;
MGLFTVTKKA TTPFDGQKPG TSGLRKKVTV FQQPHYLQNF VQSTFNALPV DQVRGATIVV
SGDGRYFSKD AVQIITKMAA ANGVRRVWVG QNSLMSTPAV SAVIRERVGA DGSKATGAFI
LTASHNPGGP KEDFGIKYNM GNGGPAPESV TDKIFSNTTT ISEYLISEDL PDVDISVVGV
TSFSGPEGPF DVDVFDSSVD 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 SLSDVNKLVK
EIRSDVSEVV AADEFEYKDP VDGSVSKHQG IRYLFGDGSR LVFRLSGTGS VGATIRVYIE
QYERDSSKTG RDSQDALAPL VDVALKLSKM QEYTGRSAPT VIT
//
