GPMI_ONCVO
ID GPMI_ONCVO Reviewed; 515 AA.
AC I6LDA6;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000305|PubMed:17897734};
DE Short=iPGM {ECO:0000303|PubMed:17897734};
DE EC=5.4.2.12 {ECO:0000269|PubMed:17897734};
DE AltName: Full=Cofactor-independent phosphoglycerate mutase homolog {ECO:0000303|PubMed:17897734};
GN Name=ipgm-1 {ECO:0000250|UniProtKB:G5EFZ1};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282 {ECO:0000312|EMBL:AAV33247.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=17897734; DOI=10.1016/j.molbiopara.2007.08.002;
RA Raverdy S., Zhang Y., Foster J., Carlow C.K.;
RT "Molecular and biochemical characterization of nematode cofactor
RT independent phosphoglycerate mutases.";
RL Mol. Biochem. Parasitol. 156:210-216(2007).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000269|PubMed:17897734}.
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; Evidence={ECO:0000269|PubMed:17897734};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17897734};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17897734};
CC Note=Binds 2 manganese or magnesium ions per subunit (By similarity).
CC Cobalt and nickel are less efficient (PubMed:17897734).
CC {ECO:0000250|UniProtKB:Q9X519, ECO:0000269|PubMed:17897734};
CC -!- ACTIVITY REGULATION: Activity is not affected by 2,3-
CC bisphosphoglycerate. {ECO:0000269|PubMed:17897734}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.301 mM for 3-phosphoglycerate {ECO:0000269|PubMed:17897734};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:17897734};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius. Active between 17 and 32
CC degrees Celsius. {ECO:0000269|PubMed:17897734};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000305|PubMed:17897734}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; AY640434; AAV33247.1; -; mRNA.
DR AlphaFoldDB; I6LDA6; -.
DR SMR; I6LDA6; -.
DR STRING; 6282.I6LDA6; -.
DR HOGENOM; CLU_026099_2_0_1; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000024404; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 HAMAP; MF_01038; GpmI; 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 Glycolysis; Isomerase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..515
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431788"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 259..262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 401
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 405
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 442
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 443
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 460
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
SQ SEQUENCE 515 AA; 57217 MW; 3004013CCA7048B9 CRC64;
MSEVKNRVCL VVIDGWGISN ESKGNAILNA KTPVMDELCA LNSHPIEAHG LHVGLPEGLM
GNSEVGHLNI GAGRVVYQDI VRINLAVKNK TLVENKHLKE AAERAIKGNG RIHLCGLVSD
GGVHSHIDHL FALITALKQL KVPQLYIHFF GDGRDTSPTS GVGFLQQLID FVNKEQYGEI
ATIVGRYYAM DRDKRWERIR VCYDALIAGV GEKTTIDKAI DVIKGRYAKD ETDEFLKPII
LSDKGRTKDG DTLIFFDYRA DRMREITECM GMERYKDLKS DIKHPKDMQV IGMTQYKAEF
TFPALFPPES HKNVLAEWLS VKGLTQFHCA ETEKYAHVTF FFNGGVEKQF ENEERCLVPS
PKVATYDLEP AMSSAGVADK MIEQLNRKAH AFIMCNFAPP DMVGHTGVYE AAVKAVEATD
IAIGRIYEAC KKNDYVLMVT ADHGNAEKMI APDGGKHTAH TCNLVPFTCS SLKFKFMDKL
PDREMALCDV APTVLKVLGL PLPSEMTGKP VVIEV
