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Database: UniProt
Entry: A0A0L0D5X9_THETB
LinkDB: A0A0L0D5X9_THETB
Original site: A0A0L0D5X9_THETB 
ID   A0A0L0D5X9_THETB        Unreviewed;       290 AA.
AC   A0A0L0D5X9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
GN   ORFNames=AMSG_02610 {ECO:0000313|EMBL:KNC47585.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC47585.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC47585.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC47585.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) 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}.
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DR   EMBL; GL349447; KNC47585.1; -; Genomic_DNA.
DR   RefSeq; XP_013759515.1; XM_013904061.1.
DR   AlphaFoldDB; A0A0L0D5X9; -.
DR   STRING; 461836.A0A0L0D5X9; -.
DR   EnsemblProtists; KNC47585; KNC47585; AMSG_02610.
DR   GeneID; 25562276; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   OMA; TGWHDVP; -.
DR   OrthoDB; 1008469at2759; -.
DR   Proteomes; UP000054408; 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   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:UP000054408}.
FT   ACT_SITE        40
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        118
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         39..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         52..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         118..121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         145..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         214..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            213
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   290 AA;  31110 MW;  F541EA9715F4CBBB CRC64;
     MLAATMRAAS AATTSAATAT AATAATASAR WAHTLVLLRH GQSQWNLENR FTGWVDVALT
     DDGRKEAATA GAAMAAAGLE FDAAYTSVLK RAISTLNIAL EVMGSEWLPV SRSWRLNERH
     YGALSGLNKA ETADKFGEDQ VLVWRRSYDV PPPLLDTDSP YWPGHDRRYA GLDSDILPRG
     ECLKDTVERI MPLWEGEMGP AIAAGQRLVV AAHGNSIRAL VKHLDNIDDN DILGINIPTG
     VPLVYTLDDS LRPIRQENSA GLLSGVYLGD PDEVAAAAEA VRNQSAATAH
//
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