PMGI_MAIZE
ID PMGI_MAIZE Reviewed; 559 AA.
AC P30792;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
DE Short=BPG-independent PGAM;
DE Short=Phosphoglyceromutase;
DE EC=5.4.2.12;
DE AltName: Full=PGAM-I;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1535626; DOI=10.1016/s0021-9258(18)42346-0;
RA Grana X., de Lecea L., El-Maghrabi M.R., Urena J.M., Caellas C.,
RA Carreras J., Puigdomenech P., Pilkis S.J., Climent F.;
RT "Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-
RT independent phosphoglycerate mutase from maize. Possible relationship to
RT the alkaline phosphatase family.";
RL J. Biol. Chem. 267:12797-12803(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 22;
RX PubMed=8093040; DOI=10.1006/bbrc.1994.2310;
RA Perez de la Ossa P., Grana X., Ruiz-Lozano P., Climent F.;
RT "Isolation and characterization of cofactor-independent phosphoglycerate
RT mutase gene from maize.";
RL Biochem. Biophys. Res. Commun. 203:1204-1209(1994).
RN [3]
RP PROTEIN SEQUENCE OF 223-236.
RC TISSUE=Coleoptile;
RX AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C.,
RA Zivy M., de Vienne D.;
RT "The maize two dimensional gel protein database: towards an integrated
RT genome analysis program.";
RL Theor. Appl. Genet. 93:997-1005(1996).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Found ubiquitously in germinating seed.
CC -!- DEVELOPMENTAL STAGE: Expression most important during germination, it
CC decreases during development.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; M80912; AAA33499.1; -; mRNA.
DR EMBL; Z33611; CAA83914.1; -; Genomic_DNA.
DR EMBL; Z33612; CAA83914.1; JOINED; Genomic_DNA.
DR PIR; A42807; A42807.
DR RefSeq; NP_001105584.1; NM_001112114.1.
DR RefSeq; XP_008655440.1; XM_008657218.1.
DR AlphaFoldDB; P30792; -.
DR SMR; P30792; -.
DR STRING; 4577.GRMZM5G833389_P02; -.
DR iPTMnet; P30792; -.
DR PaxDb; P30792; -.
DR PRIDE; P30792; -.
DR GeneID; 542578; -.
DR KEGG; zma:542578; -.
DR MaizeGDB; 30148; -.
DR eggNOG; KOG4513; Eukaryota.
DR OrthoDB; 304612at2759; -.
DR BioCyc; MetaCyc:MON-9165; -.
DR SABIO-RK; P30792; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P30792; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Isomerase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..559
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212110"
FT ACT_SITE 81
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 28
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 170..171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 286..289
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 430
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 434
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 501
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT CONFLICT 21
FT /note="S -> P (in Ref. 2; CAA83914)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="W -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 493..494
FT /note="DR -> GG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 60620 MW; 52D1FA3388A7A21A CRC64;
MGSSGFSWTL PDHPKLPKGK SVAVVVLDGW GEANPDQYNC IHVAQTPVMD SLKNGAPEKW
RLVKAHGTAV GLPSDDDMGN SEVGHNALGA GRIFAQGAKL VDQALASGKI YDGDGFNYIK
ESFESGTLHL IGLLSDGGVH SRLDQLQLLL KGVSERGAKK IRVHILTDGR DVLDGSSIGF
VETLENDLLE LRAKGVDAQI ASGGGRMYVT MDRYENDWDV VKRGWDAQVL GEAPYKFKSA
LEAVKTLRAQ PKANDQYLPP FVIVDDSGNA VGPVLDGDAV VTINFRADRM VMLAKALEYA
DFDNFDRVRV PKIRYAGMLQ YDGELKLPSR YLVSPPEIDR TSGEYLVKNG IRTFACSETV
KFGHVTFFWN GNRSGYFDAT KEEYVEVPSD SGITFNVAPN MKALEIAEKA RDALLSGKFD
QVRVNLPNGD MVGHTGDIEA TVVACKAADE AVKIILDAVE QVGGIYLVTA DHGNAEDMVK
RNKSGKPLLD KNDRIQILTS HTLQPVPVAI GGPGLHPGVK FRNDIQTPGL ANVAATVMNL
HGFEAPADYE QTLIEVADN
