ID PMGI_RICCO Reviewed; 556 AA.
AC P35493;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 27-MAR-2024, entry version 112.
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 Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-12.
RC STRAIN=cv. Baker 296; TISSUE=Endosperm;
RX PubMed=8260624; DOI=10.1007/bf00021818;
RA Huang Y., Blakeley S.D., McAleese S.M., Fothergill-Gilmore L.A.,
RA Dennis D.T.;
RT "Higher-plant cofactor-independent phosphoglyceromutase: purification,
RT molecular characterization and expression.";
RL Plant Mol. Biol. 23:1039-1053(1993).
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 -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; X70652; CAA49995.1; -; mRNA.
DR PIR; S49647; S49647.
DR AlphaFoldDB; P35493; -.
DR SMR; P35493; -.
DR eggNOG; KOG4513; Eukaryota.
DR UniPathway; UPA00109; UER00186.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
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; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 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 NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Isomerase; Manganese;
KW Metal-binding.
FT CHAIN 1..556
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212113"
FT ACT_SITE 78
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 25
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 167..168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 283..286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 427
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 431
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 468
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 469
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 498
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
SQ SEQUENCE 556 AA; 60818 MW; F6456D7D8067862C CRC64;
GEFTWKLADH PKLPKGKTIA MVVLDGWGEA KPDQYNCIHV AETPTMDSFK KTAPERWRLI
KAHGTAVGLP TEDDMGNSEV GHNALGAGRI YAQGAKLVDL ALASGKIYEG EGFKYVKECF
DKGTLHLIGL LSDGGVHSRL DQLQLLLKGA AEHGAKRIRV HVLTDGRDVI DGTSVGFAET
LEKDLENLRE KGVDAQVASG GGRMYVTMDR YENDWNVVKR GWDAQVLGEA PYKFKSAVEA
IKKLREEPKA NDQYLPPFVI VDENGKPVGP IVDGDAVVTI NFRADRMVML AKALEYENFD
TFDRVRFPKI HYAGMLQYDG ELKLPSHYLV SPPEIERTSG EYLVHNGVHT FACSETVKFG
HVTFFWNGNR SGYFNPEMEE YVEIPSDVGI TFNVQPKMKA IEIAEKARDA ILSGKFQQVR
VNIPNGDMVG HTGDVEATVV GCKAADEAVK MIIDAIEQVG GIYVVTADHG NAEDMVKRDK
SGKPMADKSG KIQILTSHTL QPVPIAIGGP GLTPGVRFRS DIPTGGLANV AATVMNLHGF
EAPSDYEPTL IEAVDN
//
