ID A0A0G0LIC8_9BACT Unreviewed; 349 AA.
AC A0A0G0LIC8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN ORFNames=UT15_C0003G0002 {ECO:0000313|EMBL:KKQ90827.1};
OS Berkelbacteria bacterium GW2011_GWA1_39_10.
OC Bacteria; Candidatus Berkelbacteria.
OX NCBI_TaxID=1618332 {ECO:0000313|EMBL:KKQ90827.1, ECO:0000313|Proteomes:UP000033862};
RN [1] {ECO:0000313|EMBL:KKQ90827.1, ECO:0000313|Proteomes:UP000033862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000256|ARBA:ARBA00008819}.
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:KKQ90827.1}.
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DR EMBL; LBVS01000003; KKQ90827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0LIC8; -.
DR STRING; 1618332.UT15_C0003G0002; -.
DR PATRIC; fig|1618332.3.peg.121; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000033862; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..112
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT DOMAIN 121..330
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 349 AA; 39525 MW; 2DEA5C1DCC4C7DE8 CRC64;
MYAMDRDHHW DRTIQVFKML VEGNAPAAES IEKAITQNYK KGLEDGAIEP TLIKDQNVKV
TIKPNDVILF FNFRPDRARQ LTEIFVNTDF RHFFWKPQVP VNLLFSSLTK YSRKFNTQIA
FPRKMISNIL PEVLSKYHKN DLRIAESEKR AHVTYFFNCG REEPFKFETR KIFASPDTDN
YDQTPAMSGR QITQAAITAI GQNTDFILIN FANVDLIAHT GNIIAAGQAV LKVDLFVKEI
VESNLRAGGA TIITADHGNV EQMVSISKNV EQETHHTFNP VPFILIAKDK KKNLIQGALS
ASANTLSKIL SAKNTLADVA PTVLEIMNLP KPVVLKVRFI RLIPKQIKF
//
