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Database: UniProt
Entry: A0A117MIB2_9EURY
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ID   A0A117MIB2_9EURY        Unreviewed;       411 AA.
AC   A0A117MIB2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=XE10_0061 {ECO:0000313|EMBL:KUL05657.1};
OS   Methanoculleus marisnigri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=2198 {ECO:0000313|EMBL:KUL05657.1, ECO:0000313|Proteomes:UP000054598};
RN   [1] {ECO:0000313|Proteomes:UP000054598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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}.
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:KUL05657.1}.
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DR   EMBL; LGHE01000003; KUL05657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117MIB2; -.
DR   PATRIC; fig|2198.3.peg.1460; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000054598; Unassembled WGS sequence.
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}.
FT   DOMAIN          5..401
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   411 AA;  43435 MW;  E5D9E769B9E0549E CRC64;
     MIAHKVLFLV LDGISDRPCE ALDGLTPLAA ARTPVLDRIA GEGVCGIMDT IAPGIRPGSD
     TSHLALLGYP PQEYYTGRGP LEAEGTGISM TAGMIGFRCN FATVDADGLV TDRRAGRISR
     TQPLSEAIRD GVDLSPLGLG FRLESGAGHR AALALTGEGL GDKVSSNDPK KEGVRPLTIR
     SCTDDAADVK TAVACNEFIR QSSKILFEHP LNLRRMEEGV PPANFLLIRG AGKMGAFPQF
     SERYELSGSV ISAATLISGI GKVVGLEHIP VPGTTGSVDS DLNAKVKAAI GELGRKDFVL
     MNIKGADEAG HDGKGIQKRD FIEVIDAALE PLLTLSDTLL VVCADHSTPC SIKDHSADPV
     PVVIRGPGVR TDRTTRFDEV SCAEGGLHRI RGCDLMPIAL DLINKSHKYG A
//
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