ID A0A162PC72_9CRUS Unreviewed; 253 AA.
AC A0A162PC72;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
DE EC=5.4.2.4 {ECO:0000256|RuleBase:RU004511};
GN ORFNames=APZ42_015250 {ECO:0000313|EMBL:KZS18722.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS18722.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS18722.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS18722.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS18722.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|ARBA:ARBA00000380,
CC ECO:0000256|RuleBase:RU004511};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000505,
CC ECO:0000256|RuleBase:RU004511};
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC ECO:0000256|RuleBase:RU004511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS18722.1}.
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DR EMBL; LRGB01000512; KZS18722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162PC72; -.
DR STRING; 35525.A0A162PC72; -.
DR EnsemblMetazoa; XM_032942503.2; XP_032798394.2; LOC116935138.
DR EnsemblMetazoa; XM_045167891.1; XP_045023826.1; LOC116935138.
DR OrthoDB; 1008469at2759; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU004511};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 9..16
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 253 AA; 28543 MW; E0C9FA98162656FD CRC64;
MVYKIVMVRH GESAWNKENR FCGWFDADLS ENGVKEAHAA GKALKEAGYH FDVAHTSALT
RAQITLQTIL EELGQTDIPV HKTWRLNERH YGGLTGLNKT ETAAKHGEAQ VQIWRRSFDV
PPPPLEESSE FYKIIMDDPR YAVEPSKDEF PLFESLKLTI QRTLPYWNDV IVPQIKEGKS
ILIAAHGNSL RGIVKHLDNM SEDAIMGLNL PTGIPFVYEL DENLKPITSM QFLGDEETVR
KAMEAVANQG KAK
//
