ID E0SH35_DICD3 Unreviewed; 216 AA.
AC E0SH35;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=ytjC {ECO:0000313|EMBL:ADN00128.1};
GN Synonyms=gpmB {ECO:0000256|HAMAP-Rule:MF_01040};
GN OrderedLocusNames=Dda3937_00399 {ECO:0000313|EMBL:ADN00128.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00128.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADN00128.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADN00128.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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; CP002038; ADN00128.1; -; Genomic_DNA.
DR RefSeq; WP_013319547.1; NC_014500.1.
DR AlphaFoldDB; E0SH35; -.
DR STRING; 198628.Dda3937_00399; -.
DR GeneID; 9735407; -.
DR KEGG; ddd:Dda3937_00399; -.
DR PATRIC; fig|198628.6.peg.3870; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_5_6; -.
DR OrthoDB; 9783269at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:ADN00128.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006859};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 83
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 83..86
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040"
FT BINDING 152..153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040"
FT SITE 151
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01040"
SQ SEQUENCE 216 AA; 24190 MW; 8895EA0409EA3BFE CRC64;
MLQVYLVRHG ETEWNVARRI QGQSDSPLTL GGEHQARLVA ERVKKLGITH IFTSDLGRTR
RTADIISQAC GNCPVIMEPS LRELNMGVLE ERLIDSLSPE EERWRKQLVD GTRDGRIPDG
ESMSELALRM QRVLTKCLAL PEGSRPLLVS HGIALGCLLS TLLGLPAWAE RRLRLRNCSL
SRVDYQQSPW LAPGWIVETA GDISHLDAPA LDELQR
//
