GPMI_CAEEL
ID GPMI_CAEEL Reviewed; 539 AA.
AC G5EFZ1; Q8IA68;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
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:0000312|WormBase:F57B10.3a};
GN Name=ipgm-1 {ECO:0000312|WormBase:F57B10.3a};
GN ORFNames=F57B10.3 {ECO:0000312|WormBase:F57B10.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAT01444.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP 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=0.508 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 22 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F57B10.3a};
CC IsoId=G5EFZ1-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F57B10.3b};
CC IsoId=G5EFZ1-2; Sequence=VSP_057382;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. High expression levels in
CC the nerve ring region, intestine and body wall muscles.
CC {ECO:0000269|PubMed:15234973}.
CC -!- DISRUPTION PHENOTYPE: RNAi knockdown results in embryonic lethality.
CC The few surviving larvae have sluggish movements, abnormal body
CC morphology, developmental arrest and impaired survival.
CC {ECO:0000269|PubMed:15234973}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000305}.
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DR EMBL; AY594354; AAT01444.1; -; mRNA.
DR EMBL; FO081416; CCD71471.1; -; Genomic_DNA.
DR EMBL; FO081416; CCD71472.1; -; Genomic_DNA.
DR PIR; T32749; T32749.
DR RefSeq; NP_491896.1; NM_059495.4. [G5EFZ1-1]
DR RefSeq; NP_871851.1; NM_182051.3. [G5EFZ1-2]
DR PDB; 5KGL; X-ray; 2.45 A; A/B=1-539.
DR PDB; 5KGM; X-ray; 2.95 A; A/B=1-539.
DR PDB; 5KGN; X-ray; 1.95 A; A/B=19-539.
DR PDB; 7KNF; X-ray; 1.80 A; A/B=19-539.
DR PDB; 7KNG; X-ray; 2.10 A; A/B=19-539.
DR PDBsum; 5KGL; -.
DR PDBsum; 5KGM; -.
DR PDBsum; 5KGN; -.
DR PDBsum; 7KNF; -.
DR PDBsum; 7KNG; -.
DR AlphaFoldDB; G5EFZ1; -.
DR SMR; G5EFZ1; -.
DR STRING; 6239.F57B10.3a; -.
DR EPD; G5EFZ1; -.
DR PaxDb; G5EFZ1; -.
DR PeptideAtlas; G5EFZ1; -.
DR EnsemblMetazoa; F57B10.3a.1; F57B10.3a.1; WBGene00019001. [G5EFZ1-1]
DR EnsemblMetazoa; F57B10.3b.1; F57B10.3b.1; WBGene00019001. [G5EFZ1-2]
DR GeneID; 172376; -.
DR KEGG; cel:CELE_F57B10.3; -.
DR UCSC; F57B10.3a; c. elegans.
DR CTD; 172376; -.
DR WormBase; F57B10.3a; CE11302; WBGene00019001; ipgm-1. [G5EFZ1-1]
DR WormBase; F57B10.3b; CE33113; WBGene00019001; ipgm-1. [G5EFZ1-2]
DR eggNOG; KOG4513; Eukaryota.
DR InParanoid; G5EFZ1; -.
DR OMA; FMDGRDT; -.
DR OrthoDB; 304612at2759; -.
DR PhylomeDB; G5EFZ1; -.
DR BRENDA; 5.4.2.12; 1045.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:G5EFZ1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019001; Expressed in germ line (C elegans) and 4 other tissues.
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; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:WormBase.
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 3D-structure; Alternative splicing; Glycolysis; Isomerase; Magnesium;
KW Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..539
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431787"
FT ACT_SITE 86
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 177..178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 284..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
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 467
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 468
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 485
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057382"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5KGN"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7KNF"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:7KNF"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:5KGN"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:7KNF"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:5KGN"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:7KNF"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 399..412
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:7KNF"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 434..458
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:7KNF"
FT HELIX 514..522
FT /evidence="ECO:0007829|PDB:7KNF"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:7KNF"
SQ SEQUENCE 539 AA; 59225 MW; D52AF11E9D647D68 CRC64;
MFVALGAQIY RQYFGRRGMA MANNSSVANK VCLIVIDGWG VSEDPYGNAI LNAQTPVMDK
LCSGNWAQIE AHGLHVGLPE GLMGNSEVGH LNIGAGRVIY QDIVRINLAV KNNKFVTNES
LVDACDRAKN GNGRLHLAGL VSDGGVHSHI DHMFALVKAI KELGVPELYL HFYGDGRDTS
PNSGVGFLEQ TLEFLEKTTG YGKLATVVGR YYAMDRDNRW ERINVAYEAM IGGVGETSDE
AGVVEVVRKR YAADETDEFL KPIILQGEKG RVQNDDTIIF FDYRADRMRE ISAAMGMDRY
KDCNSKLAHP SNLQVYGMTQ YKAEFPFKSL FPPASNKNVL AEWLAEQKVS QFHCAETEKY
AHVTFFFNGG LEKQFEGEER CLVPSPKVAT YDLQPEMSAA GVADKMIEQL EAGTHPFIMC
NFAPPDMVGH TGVYEAAVKA CEATDIAIGR IYEATQKHGY SLMVTADHGN AEKMKAPDGG
KHTAHTCYRV PLTLSHPGFK FVDPADRHPA LCDVAPTVLA IMGLPQPAEM TGVSIVQKI
