ID A0A0S8EQ69_9BACT Unreviewed; 401 AA.
AC A0A0S8EQ69;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KPK49652.1};
GN ORFNames=AMK72_04000 {ECO:0000313|EMBL:KPK49652.1};
OS Planctomycetes bacterium SM23_25.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704028 {ECO:0000313|EMBL:KPK49652.1, ECO:0000313|Proteomes:UP000052058};
RN [1] {ECO:0000313|EMBL:KPK49652.1, ECO:0000313|Proteomes:UP000052058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_25 {ECO:0000313|EMBL:KPK49652.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
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 -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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:KPK49652.1}.
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DR EMBL; LJTY01000055; KPK49652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EQ69; -.
DR PATRIC; fig|1704028.3.peg.442; -.
DR Proteomes; UP000052058; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
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}.
FT DOMAIN 13..390
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 401 AA; 42376 MW; 01E6E485374E100C CRC64;
MDLTALLHDN GSKIILFVWD GVGGVQAGPD TLTELQAART PNADRLVAAG CCGLLEPVYP
GVTPGSGPGH LGLFGYDPVA FQIGRGALEA AGVGFDLRPG DVAARLNFCT LDSGGNICDR
RAGRLPDAEC RRVVAKLANA VGAVGGIEVH WTPVKEHRAL LVLRGEGLGD GLEDTDPQQT
GVPPLDVRVK DDSPRTARTA KAVRQVLARA REVLADETKA NMVLARGFAE RPTWPSVRER
FGLRAAVVAG TPMYRGVARL VGMEALDATN DVAKDVASLA AAWNDFDFFF IHYKHTDKAG
EDGDFEAKVK CIEEADAALP ALEALRPDVL TVTADHSTPS AMKAHSWHPV PVLLSAATAR
RDAVTAFDEV ACIQGGLGLR PSTHLMPLAL AHAGRLAKFG A
//
