GPMA_NEIG2
ID GPMA_NEIG2 Reviewed; 227 AA.
AC B4RIY7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; OrderedLocusNames=NGK_0248;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
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:0000255|HAMAP-Rule:MF_01039};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01039}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; CP001050; ACF28942.1; -; Genomic_DNA.
DR RefSeq; WP_003689726.1; NC_011035.1.
DR PDB; 5UM0; X-ray; 1.85 A; A/B/C/D=1-227.
DR PDBsum; 5UM0; -.
DR AlphaFoldDB; B4RIY7; -.
DR SMR; B4RIY7; -.
DR EnsemblBacteria; ACF28942; ACF28942; NGK_0248.
DR GeneID; 66752455; -.
DR KEGG; ngk:NGK_0248; -.
DR HOGENOM; CLU_033323_1_5_4; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 1122642at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002564; Chromosome.
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; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..227
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_1000135960"
FT ACT_SITE 8
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 7..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 20..21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:5UM0"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:5UM0"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:5UM0"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:5UM0"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5UM0"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5UM0"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:5UM0"
SQ SEQUENCE 227 AA; 25929 MW; 0EBB181FF18A1F76 CRC64;
MELVFIRHGQ SEWNAKNLFT GWRDVKLSEQ GLAEAAAAGK KLKENGYEFD IAFTSVLTRA
IKTCNIVLEE SDQLFVPQIK TWRLNERHYG RLQGLDKKQT AEKYGDEQVR IWRRSYDTLP
PLLDKDDAFS AHKDRRYAHL PADVVPDGEN LKVTLERVLP FWEDQIAPAI LSGKRVLVAA
HGNSLRALAK HIEGISDEDI MGLEIPTGQP LVYKLDDNLK VIEKFYL
