ID A0A023BB42_GRENI Unreviewed; 249 AA.
AC A0A023BB42;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
GN ORFNames=GNI_028430 {ECO:0000313|EMBL:EZG79197.1};
OS Gregarina niphandrodes (Septate eugregarine).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC Eugregarinorida; Gregarinidae; Gregarina.
OX NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG79197.1, ECO:0000313|Proteomes:UP000019763};
RN [1] {ECO:0000313|EMBL:EZG79197.1, ECO:0000313|Proteomes:UP000019763}
RP NUCLEOTIDE SEQUENCE.
RA Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA Brunk B., Roos D., Caler E., Lorenzi H.;
RL Submitted (DEC-2013) 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 -!- 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:EZG79197.1}.
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DR EMBL; AFNH02000212; EZG79197.1; -; Genomic_DNA.
DR RefSeq; XP_011129112.1; XM_011130810.1.
DR AlphaFoldDB; A0A023BB42; -.
DR EnsemblProtists; EZG79197; EZG79197; GNI_028430.
DR GeneID; 22911232; -.
DR VEuPathDB; CryptoDB:GNI_028430; -.
DR eggNOG; KOG0235; Eukaryota.
DR OMA; RMLPYWY; -.
DR OrthoDB; 1008469at2759; -.
DR Proteomes; UP000019763; Unassembled WGS sequence.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate 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:UP000019763}.
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 22..23
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 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 183
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 249 AA; 28153 MW; 96B039E2822E1ED6 CRC64;
MVYKLVLVRH GESTWNKENR FTGWTDVPLS ETGRQEALAA AEVLAAKGYK FDVAFTSVLK
RAVTTCWSVL ENTDQCAVPV EQSWRLNERH YGALQGLNKA ETAEKHGEAQ VKIWRRSYDV
CPPALETSDE RFPGNQALYS KLPKDCLPQT ESLKTCIDRV LPYWQDTIAP QVLDGKNVLI
AAHGNSLRGL VKHLDQMTEE QVLELNIPTG VPLVYELDEN LKPIKHYYLM DEAELKARMD
AVANQGKKQ
//
