ID A0A0U3EC29_9CREN Unreviewed; 412 AA.
AC A0A0U3EC29;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01402};
DE Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01402};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01402};
DE Short=aPGAM {ECO:0000256|HAMAP-Rule:MF_01402};
DE EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01402};
GN Name=apgM {ECO:0000256|HAMAP-Rule:MF_01402};
GN ORFNames=EYM_07205 {ECO:0000313|EMBL:ALU12019.1};
OS Ignicoccus islandicus DSM 13165.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=940295 {ECO:0000313|EMBL:ALU12019.1, ECO:0000313|Proteomes:UP000060778};
RN [1] {ECO:0000313|EMBL:ALU12019.1, ECO:0000313|Proteomes:UP000060778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13165 {ECO:0000313|EMBL:ALU12019.1,
RC ECO:0000313|Proteomes:UP000060778};
RA Podar M.;
RT "Comparative genomics of Ignicoccus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000370,
CC ECO:0000256|HAMAP-Rule:MF_01402};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798,
CC ECO:0000256|HAMAP-Rule:MF_01402}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524,
CC ECO:0000256|HAMAP-Rule:MF_01402}.
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DR EMBL; CP006867; ALU12019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3EC29; -.
DR STRING; 940295.EYM_07205; -.
DR KEGG; iis:EYM_07205; -.
DR PATRIC; fig|940295.4.peg.1400; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000060778; 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; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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 NCBIfam; TIGR00306; apgM; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01402};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01402};
KW Reference proteome {ECO:0000313|Proteomes:UP000060778}.
FT DOMAIN 1..402
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 412 AA; 44528 MW; E167AB0DCFAC99DD CRC64;
MVLIVGDGMG DRLVPSLNYK TPLQEASTPN LDEMARRGQT GLINVIAPGI PPGSDTAHIS
LFGLDPFLWY EGRGPFEAMG VGASLTKGDV ALRGNFATVK EEGGKLIVVD RRAGRKVDEA
SELVEVLNEK LNEVDGVKVE FYHATEHRLA VVLRGEGLSD KVSDTDPHEV GKPVLESRPL
EDTPEAKKTA EVLTKITFKS YEVLKDHPAN KRRIEKGLPP ANIVLLRGAG MLRKPLPTLQ
ERIGVKAAAV GATALVLGVA KAVGMDLYTP PGATGGVDTD YKSKARKAVE LLKDYDMVFV
HLKGTDAASH DGLVEEKVRM IEALDYIAGY IMDYYDGEAV FVVTPDHATP VTVKEHTGDP
VPSLLYAPTA IPDDTKEYNE ISVAKGKLSG IRGMDLFNLM VNYANRAKKF GA
//
