GPMB_PHOLL
ID GPMB_PHOLL Reviewed; 215 AA.
AC Q7N900;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable phosphoglycerate mutase GpmB {ECO:0000255|HAMAP-Rule:MF_01040};
DE EC=5.4.2.- {ECO:0000255|HAMAP-Rule:MF_01040};
DE AltName: Full=PGAM {ECO:0000255|HAMAP-Rule:MF_01040};
DE AltName: Full=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01040};
GN Name=gpmB {ECO:0000255|HAMAP-Rule:MF_01040}; OrderedLocusNames=plu0559;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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:0000255|HAMAP-Rule:MF_01040};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01040}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01040}.
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DR EMBL; BX571860; CAE12854.1; -; Genomic_DNA.
DR RefSeq; WP_011144941.1; NC_005126.1.
DR AlphaFoldDB; Q7N900; -.
DR SMR; Q7N900; -.
DR STRING; 243265.plu0559; -.
DR EnsemblBacteria; CAE12854; CAE12854; plu0559.
DR GeneID; 24168092; -.
DR KEGG; plu:plu0559; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_5_6; -.
DR OMA; TEWNVAR; -.
DR OrthoDB; 1122642at2; -.
DR BioCyc; PLUM243265:PLU_RS02760-MON; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002514; 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; -; 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 Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..215
FT /note="Probable phosphoglycerate mutase GpmB"
FT /id="PRO_0000179949"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT BINDING 82..85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT SITE 150
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
SQ SEQUENCE 215 AA; 24059 MW; 2228D9A465E94A3E CRC64;
MLQVYLVRHG ESEWNAARRI QGQSDSPLTE TGEHQARLVA QRVKSESITH IITSDLGRTR
RTAEIIAKVC GCEIILEPRL RELHMGVLER RNIDSLTSEE EKWRKKVLDG TPGGRIPKGE
SMDELAVRMR AALENCRNLP VGSRPLLVSH GIALGCLVGT ILGLPAHAER RLRLRNCSLS
RVDYQHSPWL ASGWIVETAG DITHLDTPAL DELQR
