GPMI_BRUMA
ID GPMI_BRUMA Reviewed; 515 AA.
AC Q4VWF8;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000305|PubMed:15234973};
DE Short=iPGM {ECO:0000303|PubMed:15234973};
DE EC=5.4.2.12 {ECO:0000269|PubMed:15234973, 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 Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000312|EMBL:AAQ97626.1};
RN [1] {ECO:0000312|EMBL:AAQ97626.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND PATHWAY.
RX PubMed=15234973; DOI=10.1074/jbc.m405877200;
RA Zhang Y., Foster J.M., Kumar S., Fougere M., Carlow C.K.;
RT "Cofactor-independent phosphoglycerate mutase has an essential role in
RT Caenorhabditis elegans and is conserved in parasitic nematodes.";
RL J. Biol. Chem. 279:37185-37190(2004).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
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:15234973,
CC 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:15234973,
CC 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:15234973}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.353 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:15234973}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; AY330617; AAQ97626.1; -; mRNA.
DR AlphaFoldDB; Q4VWF8; -.
DR SMR; Q4VWF8; -.
DR STRING; 6279.Q4VWF8; -.
DR EnsemblMetazoa; Bm13317.1; Bm13317.1; WBGene00233578.
DR WBParaSite; Bm13317.1; Bm13317.1; WBGene00233578.
DR BRENDA; 5.4.2.12; 997.
DR SABIO-RK; Q4VWF8; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IDA:WormBase.
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; 3.40.1450.10; -; 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_0000431789"
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; 57320 MW; FA83A4F76FE31A8F CRC64;
MAEAKNRVCL VVIDGWGISN ETKGNAILNA KTPVMDELCV MNSHPIQAHG LHVGLPEGLM
GNSEVGHLNI GAGRVVYQDI VRINLAVKNK TLVENKHLKE AAERAIKGNG RMHLCGLVSD
GGVHSHIDHL FALITALKQL KVPKLYIQFF GDGRDTSPTS GVGFLQQLID FVNKEQYGEI
STIVGRYYAM DRDKRWERIR VCYDALIGGV GEKTTIDKAI DVIKGRYAKD ETDEFLKPII
LSDEGRTKDG DTLIFFDYRA DRMREITECM GMERYKDLNS NIKHPKNMQV IGMTQYKAEF
TFPALFPPES HKNVLAEWLS VNGLTQFHCA ETEKYAHVTF FFNGGVEKQF ANEERCLVVS
PKVATYDLEP PMSSAAVADK VIEQLHMKKH PFVMCNFAPP DMVGHTGVYE AAVKAVEATD
IAIGRIYEAC KKNDYILMVT ADHGNAEKMM APDGSKHTAH TCNLVPFTCS SMKYKFMDKL
PDREMALCDV APTVLKVMGV PLPSEMTGQP LVNEA
