ID A0A068R5G3_9GAMM Unreviewed; 215 AA.
AC A0A068R5G3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:CDG22458.1};
GN ORFNames=XPG1_2811 {ECO:0000313|EMBL:CDG22458.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG22458.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG22458.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG22458.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-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}.
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DR EMBL; FO704551; CDG22458.1; -; Genomic_DNA.
DR RefSeq; WP_045959367.1; NZ_FO704551.1.
DR AlphaFoldDB; A0A068R5G3; -.
DR STRING; 1354304.XPG1_2811; -.
DR KEGG; xpo:XPG1_2811; -.
DR HOGENOM; CLU_033323_9_5_6; -.
DR OrthoDB; 9783269at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000032735; Chromosome.
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:CDG22458.1}.
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 82..85
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040,
FT ECO:0000256|PIRSR:PIRSR613078-2"
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; 23909 MW; 347F574252EE4C00 CRC64;
MLQVYLVRHG ETEWNVARRI QGQSDSPLTE TGRHQALLVA QRIKSENITH VITSDLGRAR
QTAEIIAQAC GCDVILESRL RELHMGVLEN RELSSLTPEE ESWRKSLVDG TPNGRIPEGE
SMHEVSTRMR AALENCLNLP VGSRPLLVSH GMALVSLVCS ILGLPANSER RLRLRNCSIS
RVDYQDSPWL ASGWIVETTG DITHLDMPAL DELQG
//
