ID A0A1F8N9J1_9CHLR Unreviewed; 397 AA.
AC A0A1F8N9J1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Cofactor-independent phosphoglycerate mutase {ECO:0000313|EMBL:OGO07543.1};
GN ORFNames=A2Y61_04455 {ECO:0000313|EMBL:OGO07543.1};
OS Chloroflexi bacterium RBG_13_60_13.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797635 {ECO:0000313|EMBL:OGO07543.1, ECO:0000313|Proteomes:UP000180307};
RN [1] {ECO:0000313|EMBL:OGO07543.1, ECO:0000313|Proteomes:UP000180307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO07543.1}.
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DR EMBL; MGNC01000146; OGO07543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8N9J1; -.
DR Proteomes; UP000180307; 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}.
FT DOMAIN 1..373
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 397 AA; 43274 MW; 4BDD93C6A17D3982 CRC64;
MRYAVLVGDG MADYPLEELG DRTPLEVARI PNMDEIARQG HLGSVRTIPP GMPPGSDVAT
LSILGYDPRR HYTGRGPLEA AKLGVEISPQ EVAFRCNLVT VDDGRLVDYS SGHISSAEAS
DLIGFLQREL GTESVRFHPG VSYRHICVIK DLALMHVGCT PPHDVIGQPI EKNIPAGREA
ELLRDLMIRS HRLLDGHEVN RARVRRGEKA ANMIWLWGQG GTPQIPSFKE RFGIGGGVIS
AVDLVKGIAC LIGLDSIEVP GATGYYDTDY AAKGSYAVKC LDREEFILVH VEAPDEAGHN
GDLDQKIKAI ESFDQHVVGP VMRQFGGQPG FRALVLPDHP TPIHLRTHTA EPVPFAWYGP
GLSKGGASAF SEREADVSDL IVEHGYQLME RFIAGEK
//
