PGMP_ARATH
ID PGMP_ARATH Reviewed; 623 AA.
AC Q9SCY0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphoglucomutase, chloroplastic {ECO:0000303|PubMed:10759515};
DE Short=PGM {ECO:0000305};
DE EC=5.4.2.2 {ECO:0000269|PubMed:10759515};
DE AltName: Full=Glucose phosphomutase {ECO:0000305};
DE Flags: Precursor;
GN Name=PGMP {ECO:0000303|PubMed:10759515};
GN Synonyms=PGM {ECO:0000303|PubMed:10759515};
GN OrderedLocusNames=At5g51820 {ECO:0000312|Araport:AT5G51820};
GN ORFNames=MIO24.4 {ECO:0000312|EMBL:BAB11251.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10759515; DOI=10.1104/pp.122.4.1193;
RA Periappuram C., Steinhauer L., Barton D.L., Taylor D.C., Chatson B.,
RA Zou J.;
RT "The plastidic phosphoglucomutase from Arabidopsis. A reversible enzyme
RT reaction with an important role in metabolic control.";
RL Plant Physiol. 122:1193-1199(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10954083; DOI=10.1007/pl00008698;
RA Kofler H., Haeusler R.E., Schulz B., Groener F., Fluegge U.-I., Weber A.;
RT "Molecular characterisation of a new mutant allele of the plastid
RT phosphoglucomutase in Arabidopsis, and complementation of the mutant with
RT the wild-type cDNA.";
RL Mol. Gen. Genet. 263:978-986(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose (Probable). Factor that affects seed oil content
CC (PubMed:10759515). Accumulated starch in young embryos may play an
CC important role in providing carbon resources for seed storage lipid
CC biosynthesis in oilseed plants (Probable).
CC {ECO:0000269|PubMed:10759515, ECO:0000305|PubMed:10759515}.
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:10759515};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=98.5 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:10759515};
CC Vmax=4.5 umol/min/mg enzyme with alpha-D-glucose 1-phosphate as
CC substrate {ECO:0000269|PubMed:10759515};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques and germinating
CC seeds. {ECO:0000269|PubMed:10759515}.
CC -!- DISRUPTION PHENOTYPE: Reduced oil content in seeds.
CC {ECO:0000269|PubMed:10759515}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AJ242601; CAB64725.1; -; mRNA.
DR EMBL; AF216580; AAG44095.1; -; mRNA.
DR EMBL; AB010074; BAB11251.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96131.1; -; Genomic_DNA.
DR EMBL; AY099708; AAM20559.1; -; mRNA.
DR EMBL; AY128901; AAM91301.1; -; mRNA.
DR PIR; T52656; T52656.
DR RefSeq; NP_199995.1; NM_124561.3.
DR AlphaFoldDB; Q9SCY0; -.
DR SMR; Q9SCY0; -.
DR BioGRID; 20502; 1.
DR STRING; 3702.AT5G51820.1; -.
DR iPTMnet; Q9SCY0; -.
DR MetOSite; Q9SCY0; -.
DR PaxDb; Q9SCY0; -.
DR PRIDE; Q9SCY0; -.
DR ProteomicsDB; 236407; -.
DR EnsemblPlants; AT5G51820.1; AT5G51820.1; AT5G51820.
DR GeneID; 835257; -.
DR Gramene; AT5G51820.1; AT5G51820.1; AT5G51820.
DR KEGG; ath:AT5G51820; -.
DR Araport; AT5G51820; -.
DR TAIR; locus:2165351; AT5G51820.
DR eggNOG; KOG0625; Eukaryota.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; Q9SCY0; -.
DR OMA; RGHVREK; -.
DR OrthoDB; 555015at2759; -.
DR PhylomeDB; Q9SCY0; -.
DR BioCyc; ARA:AT5G51820-MON; -.
DR BioCyc; MetaCyc:AT5G51820-MON; -.
DR BRENDA; 5.4.2.2; 399.
DR SABIO-RK; Q9SCY0; -.
DR PRO; PR:Q9SCY0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SCY0; baseline and differential.
DR Genevisible; Q9SCY0; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0009590; P:detection of gravity; IMP:TAIR.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IMP:TAIR.
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; 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; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..623
FT /note="Phosphoglucomutase, chloroplastic"
FT /id="PRO_0000023895"
FT ACT_SITE 181
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 350..351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 433..435
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 576
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT CONFLICT 439
FT /note="G -> V (in Ref. 1; CAB64725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 67989 MW; 3D4A0D8132EF90F1 CRC64;
MTSTYTRFDT VFLFSRFAGA KYSPLLPSPS FTLSTSGIHI RTKPNSRFHS IIASSSSSSV
VAGTDSIEIK SLPTKPIEGQ KTGTSGLRKK VKVFMEDNYL ANWIQALFNS LPLEDYKNAT
LVLGGDGRYF NKEASQIIIK IAAGNGVGQI LVGKEGILST PAVSAVIRKR KANGGFIMSA
SHNPGGPEYD WGIKFNYSSG QPAPETITDK IYGNTLSISE IKVAEIPDID LSQVGVTKYG
NFSVEVIDPV SDYLELMEDV FDFDLIRGLL SRSDFGFMFD AMHAVTGAYA KPIFVDNLGA
KPDSISNGVP LEDFGHGHPD PNLTYAKDLV DVMYRDNGPD FGAASDGDGD RNMVLGNKFF
VTPSDSVAII AANAQEAIPY FRAGPKGLAR SMPTSGALDR VAEKLKLPFF EVPTGWKFFG
NLMDAGKLSI CGEESFGTGS DHIREKDGIW AVLAWLSILA HRNKDTKPGD KLVSVADVVK
EYWATYGRNF FSRYDYEECE SEGANKMIEY LREILSKSKA GDVYGNYVLQ FADDFSYTDP
VDGSVASKQG VRFVFTDGSR IIFRLSGTGS AGATVRIYIE QFEPDVSKHD VDAQIALKPL
IDLALSVSKL KDFTGREKPT VIT
