ID W1JC00_9GAMM Unreviewed; 215 AA.
AC W1JC00;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Probable phosphoglycerate mutase GpmB {ECO:0000256|HAMAP-Rule:MF_01040};
DE EC=5.4.2.- {ECO:0000256|HAMAP-Rule:MF_01040};
DE AltName: Full=PGAM {ECO:0000256|HAMAP-Rule:MF_01040};
DE AltName: Full=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01040};
GN Name=gpmB {ECO:0000256|HAMAP-Rule:MF_01040,
GN ECO:0000313|EMBL:CDL87653.1};
GN ORFNames=XCR1_960008 {ECO:0000313|EMBL:CDL87653.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL87653.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL87653.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL87653.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
RL Submitted (NOV-2013) 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 Evidence={ECO:0000256|HAMAP-Rule:MF_01040};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC Rule:MF_01040}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01040}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01040}.
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:CDL87653.1}.
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DR EMBL; CBXE010000493; CDL87653.1; -; Genomic_DNA.
DR RefSeq; WP_038269674.1; NZ_NJGH01000021.1.
DR AlphaFoldDB; W1JC00; -.
DR OrthoDB; 9783269at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000019197; Unassembled WGS sequence.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; 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_01040; PGAM_GpmB; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR023086; Phosphoglycerate_mutase_GpmB.
DR PANTHER; PTHR48100:SF34; BROAD-SPECIFICITY PHOSPHATASE YOR283W; 1.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01040};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01040, ECO:0000313|EMBL:CDL87653.1}.
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040"
FT SITE 150
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040"
SQ SEQUENCE 215 AA; 23985 MW; 45484B27D7F06EB7 CRC64;
MLQVYLVRHG ETEWNVARRI QGQSDSPLTE IGRRQALLVA QRIQSENITH VITSDLGRTR
ETAEIIAKAC GCEVILEPRL REINMGVLEN RELSSLTQEE ESWRKSLVDG TPNGRIPEGE
SMNEVCSRMR AALESCLDLP TGSRPLLVSH GMALVSLIFS ILGLPANSER RLRLRNCSIS
RVDYQDSPWL ASGWIVETAG DITHLNMPAL DELQG
//
