ID A0A0R1XQJ6_9LACO Unreviewed; 228 AA.
AC A0A0R1XQJ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=FC83_GL000419 {ECO:0000313|EMBL:KRM32552.1};
OS Agrilactobacillus composti DSM 18527 = JCM 14202.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Agrilactobacillus.
OX NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM32552.1, ECO:0000313|Proteomes:UP000051236};
RN [1] {ECO:0000313|EMBL:KRM32552.1, ECO:0000313|Proteomes:UP000051236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM32552.1,
RC ECO:0000313|Proteomes:UP000051236};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM32552.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGA01000070; KRM32552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1XQJ6; -.
DR STRING; 1423734.FC83_GL000419; -.
DR PATRIC; fig|1423734.3.peg.420; -.
DR eggNOG; COG0588; Bacteria.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000051236; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051236}.
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 11..18
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 24..25
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 180
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 228 AA; 25790 MW; FAB39EEEBDA7CDD0 CRC64;
MNKMTQLVLI RHGESTANRD NVYTGWSDVP LTTTGCQEAK AIGAKLATLG IDFKACHTSV
LQRAIMTSYL VLEQLHLNDL PLFKTWRLNE RHYGALRGLN KDITREIFGK RQVARWRRGY
ASVPPLLEKA DNDRRYANLD PRAIPRGESL KMASARLQPY YQANIVPRLK QGEAQLVVAH
GSSLRALIKY VEAISDTDID GVEVQNGEAI IYDFAKDMTL SDKQRLYD
//
