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HAMAP rule MF_01038

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General rule information [?]

Accession MF_01038
Dates 19-DEC-2002 (Created)
1-JUN-2023 (Last updated, Version 42)
Name GpmI
Scope
Bacteria
Archaea
Plastid
Templates Q9X519 (GPMI_GEOSE); P39773 (GPMI_BACSU); P37689 (GPMI_ECOLI): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
GPMI
Protein name
RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Short=BPG-independent PGAM;
Short=Phosphoglyceromutase;
Short=iPGM;
EC 5.4.2.12;
Gene name
gpmI

Comments [?]

case <OC:Bacillaceae>
Function Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
else
Function Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
end case
Catalytic activity RHEA:15901: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
EC 5.4.2.12
case <FTGroup:1>
Cofactor Mn(2+)
Note: Binds 2 manganese ions per subunit.
end case
Pathway Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
case <OC:Bacteria>
Subunit Monomer.
end case
case <OG:Chloroplast>
Subcellular location Plastid, chloroplast.
end case
Similarity Belongs to the BPG-independent phosphoglycerate mutase family.

Keywords [?]

case <FTGroup:1>
end case
case <OC:Bacillaceae> and <FT:15>
end case
case <OC:Bacillaceae>
end case

Gene Ontology [?]

GO:0046537; Molecular function: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity.
case <FTGroup:1>
GO:0030145; Molecular function: manganese ion binding.
end case
GO:0006096; Biological process: glycolytic process.
case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case

Cross-references [?]

Pfam PF06415; iPGM_N; 1;
PF01676; Metalloenzyme; 1;
NCBIfam TIGR01307; Pgm_bpd_ind; 1;

Features [?]

From: GPMI_GEOSE (Q9X519)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     153     154       /ligand="substrate     R-D  
BINDING     261     264       /ligand="substrate     R-x-x-R  
ACT_SITE     62     62       Phosphoserine intermediate     S  
BINDING     12     12       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     D   1
BINDING     62     62       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     S   1
BINDING     403     403       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     D   1
BINDING     407     407       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     H   1
BINDING     444     444       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     D   1
BINDING     445     445       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     H   1
BINDING     462     462       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     H   1
BINDING     123     123       /ligand="substrate     H  
BINDING     185     185       /ligand="substrate     R  
BINDING     191     191       /ligand="substrate     [RK]  
BINDING     336     336       /ligand="substrate     K  
case <OC:Bacillaceae>
From: GPMI_BACSU (P39773)
MOD_RES     36     36       Phosphotyrosine     Y  
end case

Additional information [?]

Size range 490-552 amino acids
Related rules MF_01402 (APGM)
Fusion None
Comments Possible wrong start in METMA and in the second copy of gpmI in METAC. LEPIC and LEPIN seem to be more closely related to protozoan and plant gpmI than to bacterial orthologs; not shown in alignment.