PMGI_MESCR
ID PMGI_MESCR Reviewed; 559 AA.
AC Q42908;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
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;
GN Name=PGM1;
OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Aizoaceae; Mesembryanthemum;
OC Mesembryanthemum subgen. Cryophytum.
OX NCBI_TaxID=3544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RX PubMed=7579174; DOI=10.1007/bf00043647;
RA Forsthoefel N.R., Vernon D.M., Cushman J.C.;
RT "A salinity-induced gene from the halophyte M. crystallinum encodes a
RT glycolytic enzyme, cofactor-independent phosphoglyceromutase.";
RL Plant Mol. Biol. 29:213-226(1995).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By salt stress.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; U16021; AAA86979.1; -; mRNA.
DR PIR; S60473; S60473.
DR AlphaFoldDB; Q42908; -.
DR SMR; Q42908; -.
DR UniPathway; UPA00109; UER00186.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; 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; 3.40.1450.10; -; 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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; Isomerase; Manganese; Metal-binding;
KW Stress response.
FT CHAIN 1..559
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212111"
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"
SQ SEQUENCE 559 AA; 61183 MW; 1C1CBA32D227D640 CRC64;
MGSTEFSWKL ADHPKLPKGK TLAMVVLDGW GEASANQYNC IHVAETPTMD SLKQGAPEKW
RLIRAHGKAV GLPTEDDMGN SEVGHNALGA GRIYAQGAKL VDLALESGKI YDGEGFNYIK
ESFETNTLHL IGLLSDGGVH SRLDQLQLLL KGSAERGAKR IRVHILTDGR DVLDGSSVGF
VETLENDLAQ LRAKGVDAQI ASGGGRMYVT MDRYENDWSV VKRGWDAQVL GEAPYKFKNA
VEAVKTLRQE PKANDQYLPP FVVVDESGKA VGPIVDGDAV VTLNFRADRM VMLAKALEYE
DFDKFDRVRF PKIRYAGMLQ YDGELKLPNR YLVSPPEIER TSGEYLVHNG VRTFACSETV
KFGHVTFFWN GNRSGYFKPE MEEYVEIPSD SGITFNVQPK MKALEIAEKA RDAILSGKFD
QVRVNLPNSD MVGHTGDIEA TVVACKAADE AVKMIIDAIE QVGGIYVITA DHGNAEDMVK
RDKKGQPAMD KNGNIQILTS HTLEPVPIAI GGPGLTPGVR FRNDIPTGGL ANVAATVMNL
HGFEAPSDYE PTLIEVVSN
