ID   PMGI_PRUDU              Reviewed;         488 AA.
AC   O24246;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 106.
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;
DE   Flags: Fragment;
OS   Prunus dulcis (Almond) (Amygdalus dulcis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Texas; TISSUE=Root;
RX   PubMed=7584858; DOI=10.1016/0305-0491(95)00076-3;
RA   Grana X., Perez de la Ossa P., Broceno C., Stocker M., Garriga J.,
RA   Puigdomenech P., Climent F.;
RT   "2,3-Bisphosphoglycerate-independent phosphoglycerate mutase is conserved
RT   among different phylogenic kingdoms.";
RL   Comp. Biochem. Physiol. 112B:287-293(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   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X75020; CAA52928.1; -; mRNA.
DR   PIR; T09138; T09138.
DR   AlphaFoldDB; O24246; -.
DR   SMR; O24246; -.
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   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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Isomerase; Manganese; Metal-binding.
FT   CHAIN           <1..488
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000212112"
FT   ACT_SITE        10
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         99..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         215..218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         359
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         363
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         400
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         401
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
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   NON_TER         1
SQ   SEQUENCE   488 AA;  53395 MW;  F103633B8FCD2D2A CRC64;
     LPTEDDMGNS EVGHNALGAG RIFAQGAKLV DSALETGKLY EGEGFKYIKE SFPTNTLHLI
     GLLSDGGVHS RLDQLLLLVK GASERGAKRI RVHILTDGRD VLDGSSVGFA ETLENYLAQL
     REKGVDAQIA SGGGRMYVTM DRYENDWGVV KRGWDAQVLG EAPHKFKNAV EAIKTLRQEP
     NTSDQYLPPF VIVDENGKPV GPIVDGDAVV TFNFRADRMV MIAKALEYAD FDKFDRVRFP
     KIRYAGMLQY DGELKLPSKY LVEPPEIDRT SGEYLTYNGV RTFACSETVK FGHVTFFWNG
     NRSGYFNPQM EEYVEIPSDS GITFNVQPKM KAVEIAEKGR GAILSKKFEQ VRVNLPNSDM
     VGHTSSIEAT VVACKAADEA VKIIIDAIEQ VGGIYVVTAD HGNAEDMVKR NKKGQPLLDK
     NGNIQILTSH TLQPVPIAIG GPGLAPGVQF RKDVPNGGLA NVAATVMNLH GFEAPADYET
     TLIEVVDN
//