ID A0A0F0CU41_9BACT Unreviewed; 556 AA.
AC A0A0F0CU41;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=OMAG_001185 {ECO:0000313|EMBL:KJJ84955.1};
OS Candidatus Omnitrophus magneticus.
OC Bacteria; Candidatus Omnitrophota; Omnitrophus.
OX NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ84955.1, ECO:0000313|Proteomes:UP000033428};
RN [1] {ECO:0000313|EMBL:KJJ84955.1, ECO:0000313|Proteomes:UP000033428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ84955.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJJ84955.1}.
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DR EMBL; JYNY01000232; KJJ84955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0CU41; -.
DR PATRIC; fig|1609969.3.peg.1274; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000033428; 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 CDD; cd16010; iPGM; 1.
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 NCBIfam; TIGR01307; pgm_bpd_ind; 1.
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 PIRSF; PIRSF001492; IPGAM; 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, ECO:0000256|PIRSR:PIRSR001492-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001492-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033428}.
FT DOMAIN 29..542
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 107..329
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 87
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-1"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 177..178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 293..296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 440
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 478
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 499
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ SEQUENCE 556 AA; 62244 MW; 5520514EF655CD70 CRC64;
MCFLIFVQGE NFMNLKLEPL KNPIKRKGPV LLIIMDGIGI GKHDETDGVF TANDPCLKSL
FQGPFFTKLE AHGKAVGLPS DDDMGNSEVG HNALGAGRVF AQGAKRVNAA IEDGSMFKTD
LWQELVNRAK SGHTFHFIGL LSDGNVHSHI NHLFSMIKKL FVEGVKTVRI HALLDGRDVG
EKSALTYIEQ TENILAEINK NKGYDYKIAS GGGRMITTMD RYNADWEIVK RGWNAHVLGN
ARVFNSAKEA VETFYKEDEK ITDQYLPPFV IGEGSEPVGR IKDGDSVIFF NFRGDRAIEI
SRAFDEKQFK EFDRVFCPDF LFAGLMEYDG DLHVPARYLV SPPEIDRTIS EYLCSRGIKM
FAISETQKFG HVTYFWNGNK SGYICKEFED YFEIPSDKVR FEEAPKMKAF EITEKTIELL
KSGKYKFGRL NLANGDMVGH TAVPSAIKIA VETVDQCVSR LLSVIKELDG IAIITADHGN
SDEMFTIDKK GKHSPKTAHT LNPVPFIIYD PSYKGEYSLE RGAKQGLSNV AATIINFLGF
EKPGNYDNSL IKFLVN
//
