ID A0A0U3RUX2_9EURY Unreviewed; 236 AA.
AC A0A0U3RUX2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN ORFNames=ADU37_CDS10990 {ECO:0000313|EMBL:ALV62798.1};
OS Thermococcus sp. 2319x1.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1674923 {ECO:0000313|EMBL:ALV62798.1, ECO:0000313|Proteomes:UP000061586};
RN [1] {ECO:0000313|Proteomes:UP000061586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2319x1 {ECO:0000313|Proteomes:UP000061586};
RA Kublanov I.;
RT "Isolation and characterization of the first xylanolytic hyperthermophilic
RT euryarchaeon Thermococcus sp. 2319x1 and its multidomain cellulase.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALV62798.1, ECO:0000313|Proteomes:UP000061586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2319x1 {ECO:0000313|EMBL:ALV62798.1,
RC ECO:0000313|Proteomes:UP000061586};
RX PubMed=27199905; DOI=10.3389/fmicb.2016.00552;
RA Gavrilov S.N., Stracke C., Jensen K., Menzel P., Kallnik V., Slesarev A.,
RA Sokolova T., Zayulina K., Brasen C., Bonch-Osmolovskaya E.A., Peng X.,
RA Kublanov I.V., Siebers B.;
RT "Isolation and Characterization of the First Xylanolytic Hyperthermophilic
RT Euryarchaeon Thermococcus sp. Strain 2319x1 and Its Unusual Multidomain
RT Glycosidase.";
RL Front. Microbiol. 7:552-552(2016).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512}.
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|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC ECO:0000256|HAMAP-Rule:MF_01039}.
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DR EMBL; CP012200; ALV62798.1; -; Genomic_DNA.
DR RefSeq; WP_058946617.1; NZ_LR778300.1.
DR AlphaFoldDB; A0A0U3RUX2; -.
DR STRING; 1674923.ADU37_CDS10990; -.
DR GeneID; 55597955; -.
DR KEGG; thv:ADU37_CDS10990; -.
DR PATRIC; fig|1674923.3.peg.1085; -.
DR OrthoDB; 304253at2157; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000061586; Chromosome.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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; 2.
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 Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01039};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}.
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 109
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 109..112
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 136..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 180..181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 179
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 236 AA; 27204 MW; E693F88CBA7A9DA4 CRC64;
MSKLILIRHG ESLWNKLNLF TGWVDVPLSE RGIEEALKAG ELLRGWKIDV VFTSELVRAI
QTAMLVMSKN TSGVPKIEHE NGKMKDWGIV YGEYGKNYVP VYKSWHLNER YYGKLQGFNK
DEAKKIYGED KVLLWRRSYD IAPPGGESLK DTAERTIPYF KEKILPELEK GKNVLVSAHG
NSLRSIVMHI EKLTKEQVLK LNIPTGVPLV YEYSKGKLER IGYLYEWGYD ESLHIE
//
