APGM_PYRNV
ID APGM_PYRNV Reviewed; 411 AA.
AC B1Y9H0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=aPGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01402};
GN Name=apgM {ECO:0000255|HAMAP-Rule:MF_01402}; OrderedLocusNames=Tneu_1474;
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01402}.
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:0000255|HAMAP-Rule:MF_01402};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01402}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01402}.
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DR EMBL; CP001014; ACB40399.1; -; Genomic_DNA.
DR AlphaFoldDB; B1Y9H0; -.
DR SMR; B1Y9H0; -.
DR STRING; 444157.Tneu_1474; -.
DR EnsemblBacteria; ACB40399; ACB40399; Tneu_1474.
DR KEGG; tne:Tneu_1474; -.
DR eggNOG; arCOG01696; Archaea.
DR HOGENOM; CLU_034906_2_0_2; -.
DR OMA; IAFRCNF; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001694; Chromosome.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.30.70.2130; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01402_A; ApgM_A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR PANTHER; PTHR31209; PTHR31209; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR TIGRFAMs; TIGR00306; apgM; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase.
FT CHAIN 1..411
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_1000145452"
SQ SEQUENCE 411 AA; 44251 MW; 5832855FBD9837D7 CRC64;
MPSVLWILFD GGGDRPTGGK TPFYVAFKPV IDYFTSLGSC GILDPISPGV RPGSDTAHLA
LFGYDPYRYY TGRGAFEALG AGVDLRPGDV AFRTNLATVD ESGVVVDRRA GRYIAPEEAR
AVERLMASIG EEVGKAYGVE VLYRSTVEHR GVLVLRGPVS HKVSDTDPHK VGERIHMSEP
LDGSKEAALT AQVVNEITRR FSAAAEGLEV NKARKASGRP PINAILLRGG GYMPQIEPVK
ERYKVRAAAI AGVALIRGVA RAVGMDVYTA PGLGGTKDDV FDEAVKLAVE LMSRYDVVFL
HVKGTDSTAH DGDFRGKVSV IERLDKALSP YVDKIAGNYL VVTSDHATPV SIREHTGEPV
PFLLYGPDVV TDDVGKFSEL TCWRGALGRL RGIDVMPTLS SYLGLAEKFG E