ID A0A1X1FD00_9LACO Unreviewed; 223 AA.
AC A0A1X1FD00;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN ORFNames=FAM23169_01906 {ECO:0000313|EMBL:ORN26937.1}, GKC44_10720
GN {ECO:0000313|EMBL:MSE21694.1};
OS Lentilactobacillus parabuchneri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=152331 {ECO:0000313|EMBL:ORN26937.1, ECO:0000313|Proteomes:UP000193009};
RN [1] {ECO:0000313|EMBL:ORN26937.1, ECO:0000313|Proteomes:UP000193009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAM23169 {ECO:0000313|EMBL:ORN26937.1,
RC ECO:0000313|Proteomes:UP000193009};
RX PubMed=28261177; DOI=10.3389/fmicb.2017.00218;
RA Wuthrich D., Berthoud H., Wechsler D., Eugster E., Irmler S., Bruggmann R.;
RT "The Histidine Decarboxylase Gene Cluster of Lactobacillus parabuchneri Was
RT Gained by Horizontal Gene Transfer and Is Mobile within the Species.";
RL Front. Microbiol. 8:218-218(2017).
RN [2] {ECO:0000313|EMBL:MSE21694.1, ECO:0000313|Proteomes:UP000491237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VRA_07sq_f {ECO:0000313|EMBL:MSE21694.1,
RC ECO:0000313|Proteomes:UP000491237};
RA Vasilyev I.Y., Radchenko V., Ilnitskaya E.V.;
RT "Draft Genome Sequence of Plant Growth-Promoting Rhizosphere-Associated
RT Bacteria.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|ARBA:ARBA00000380,
CC ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC ECO:0000256|HAMAP-Rule:MF_01039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01039}.
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:ORN26937.1}.
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DR EMBL; WKKY01000554; MSE21694.1; -; Genomic_DNA.
DR EMBL; MSBD01000045; ORN26937.1; -; Genomic_DNA.
DR RefSeq; WP_057910308.1; NZ_VBSV01000012.1.
DR AlphaFoldDB; A0A1X1FD00; -.
DR STRING; 152331.FAM21731_01971; -.
DR GeneID; 69803688; -.
DR KEGG; lpar:FAM21731_01971; -.
DR OrthoDB; 9781415at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000193009; Unassembled WGS sequence.
DR Proteomes; UP000491237; Unassembled WGS sequence.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01039};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}.
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 176
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 223 AA; 25584 MW; ECED9C5AE5A0DCCD CRC64;
MPTLVIMRHG ESQANRDNIF TGWSDVSLTD KGISQAHSAG KVIAKSKLAF NDVHTSFLKR
AIMTTNIVLD EIGQNFIPEH KSWRLNERHY GGLRGKNKLK VKEQVGAKQL KIWRRSFTVV
PPLLTKRDED PRYDRYGVQI PLGESLEMAQ QRLIPYWIDQ IAPRLLDGQN QLIVAHGSTL
RALIKFLENI SDEDIPNVEV PNGKPIRYDF DDQLNIINKQ FMQ
//