ID A0A1I0LYB1_9BACT Unreviewed; 420 AA.
AC A0A1I0LYB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000313|EMBL:SEV80886.1};
GN ORFNames=SAMN04487850_0101 {ECO:0000313|EMBL:SEV80886.1};
OS Prevotella aff. ruminicola Tc2-24.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=81582 {ECO:0000313|EMBL:SEV80886.1, ECO:0000313|Proteomes:UP000199373};
RN [1] {ECO:0000313|EMBL:SEV80886.1, ECO:0000313|Proteomes:UP000199373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC2-24 {ECO:0000313|EMBL:SEV80886.1,
RC ECO:0000313|Proteomes:UP000199373};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOIQ01000001; SEV80886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0LYB1; -.
DR Proteomes; UP000199373; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
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; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR NCBIfam; TIGR00306; apgM; 1.
DR NCBIfam; TIGR02535; hyp_Hser_kinase; 1.
DR PANTHER; PTHR31209:SF4; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 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};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000199373}.
FT DOMAIN 1..392
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 420 AA; 46889 MW; 7FC88694D759E537 CRC64;
MKHIIILGDG MADLPVERLG GKTLLQYAHK PMMDLLAREG RTGRLVTVPE GFPPGSEVAN
TAILGYDLNK VYEGRGPLEA ASIGYEMADD DLAIRCNIIT LEDGKIITHN GGNLETQDAD
VLIRYLNEKL AKPINEREGC ERVKFITGIQ YRHLLVIKGG SKHIVCAPPH DHPNEEWRGL
LVKAEEGAPV EPGRLTAQQT ADLINEMILK SQELLAAHPF NQERAKRGER QANSIWPWSG
GYRPSMQTLQ QQFPQIKKGS VISAVDLIRG IGHYAGLRII EVEGATGLAD TNYEGKAEAA
IKALKDEDFV FVHVEASDEA GHDGDLELKL KTIEYLDQRL ITPIYKEVET WDEPVCIAIL
PDHLTPVEMR IHVGQPVPFL FWYRGIEPDE VLQYDEVSCV SGSYGLLKLQ EFMQELMKIE
//