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Database: UniProt
Entry: A0A0P8Z3C6_LACPN
LinkDB: A0A0P8Z3C6_LACPN
Original site: A0A0P8Z3C6_LACPN 
ID   A0A0P8Z3C6_LACPN        Unreviewed;       225 AA.
AC   A0A0P8Z3C6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=pgaM {ECO:0000313|EMBL:ODO60659.1};
GN   Synonyms=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   ORFNames=ASV54_02475 {ECO:0000313|EMBL:APD00265.1}, AVR83_02610
GN   {ECO:0000313|EMBL:AOB21888.1}, Lp19_2075
GN   {ECO:0000313|EMBL:KZU94101.1}, LPJSA22_00603
GN   {ECO:0000313|EMBL:ODO60659.1};
OS   Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1590 {ECO:0000313|EMBL:ODO60659.1, ECO:0000313|Proteomes:UP000094892};
RN   [1] {ECO:0000313|Proteomes:UP000183026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA   McLeod A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOB21888.1, ECO:0000313|Proteomes:UP000093296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF {ECO:0000313|EMBL:AOB21888.1,
RC   ECO:0000313|Proteomes:UP000093296};
RA   Petkau K., Fast D., Duggal A., Foley E.;
RT   "Comparative evaluation of the genomes of common bacterial members of the
RT   Drosophila intestinal community.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KZU94101.1, ECO:0000313|Proteomes:UP000076882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19.1 {ECO:0000313|EMBL:KZU94101.1,
RC   ECO:0000313|Proteomes:UP000076882};
RA   Martino M.E.;
RT   "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT   uncoupling from niche constraints.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ODO60659.1, ECO:0000313|Proteomes:UP000094892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSA22 {ECO:0000313|EMBL:ODO60659.1,
RC   ECO:0000313|Proteomes:UP000094892};
RA   Choi H.S.;
RT   "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT   fermented soybean paste.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:APD00265.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MF1298 {ECO:0000313|EMBL:APD00265.1};
RA   McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (AUG-2018) 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}.
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DR   EMBL; CP013753; AOB21888.1; -; Genomic_DNA.
DR   EMBL; CP013149; APD00265.1; -; Genomic_DNA.
DR   EMBL; LUXM01000033; KZU94101.1; -; Genomic_DNA.
DR   EMBL; MCOL01000001; ODO60659.1; -; Genomic_DNA.
DR   RefSeq; WP_003640923.1; NZ_WWDD01000006.1.
DR   GeneID; 77217205; -.
DR   KEGG; lpb:SH83_02605; -.
DR   PATRIC; fig|1590.142.peg.534; -.
DR   OMA; LWRRSYT; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000076882; Unassembled WGS sequence.
DR   Proteomes; UP000093296; Chromosome.
DR   Proteomes; UP000094892; Unassembled WGS sequence.
DR   Proteomes; UP000183026; Chromosome.
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            179
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   225 AA;  25625 MW;  209F01523D298432 CRC64;
     MTELVLVRHG ESTANRDNTY TGWSDVPLTA VGIAQAHQAG KRLRATGLQF GAVHTSVLKR
     AIVTANIMLS EIDQLWLPEY KTWRLNERHY GALRGQNKDV TRQEYGKAQV QQWRRSFYTV
     PPLLTPAELD HDRRYTKYGA AVEPRGESLK MAYDRIMPYW IDEIAPRLLD GQNQLVVAHG
     STLRAMIKYL EHISDTGIDG VEVANGVPIC YHLDRQLHVI GKEEY
//
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