ID A0A0S8DZT7_9BACT Unreviewed; 425 AA.
AC A0A0S8DZT7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KPK41222.1};
GN ORFNames=AMJ78_06095 {ECO:0000313|EMBL:KPK41222.1};
OS Omnitrophica WOR_2 bacterium SM23_29.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK41222.1, ECO:0000313|Proteomes:UP000050824};
RN [1] {ECO:0000313|EMBL:KPK41222.1, ECO:0000313|Proteomes:UP000050824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_29 {ECO:0000313|EMBL:KPK41222.1};
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:KPK41222.1}.
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DR EMBL; LJUB01000059; KPK41222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DZT7; -.
DR PATRIC; fig|1703776.3.peg.471; -.
DR Proteomes; UP000050824; 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; 1.
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 3..421
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 425 AA; 46501 MW; 1B37DDB39CBF9F6A CRC64;
MIYVVLDGLG DRPCKEFGGK TPLEAAEKPN MNSLLKKAKT GVVYTVGKGI APESDVAVIS
ILGYDAHKYY TGRGPLESYA EGLEVNDGDL AFRVNFATLG KDNEILDRRV GRNLTTDEAS
ALAKDINEKV KLTSYPTTFK FKNTIGHRGI LVIYRKDGKK LNAEITNTDP AYDKHGVFGV
AKAEFDNFVL EARPTSGFES DEEAIAAAKL INEFTKKSIE VLNASEINKR RISEGKLAGN
LILSRDAGDR LPKFPPIHKE YGVKFGCFVE MPVEKGIAIL TGMDVVGLPL PTGNLKDDYT
LRARKVIEVI NNYGGLYIHI KGPDEPAHDG NALKKKDSIE AIDKFFFSEL LKSIKLEKNI
IAITSDHSTP CHLKAHSDDP VPLLIASEGI ISDGTADFSE KFCAKGSLGE LEGKNLMSLF
IEFAK
//
