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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
 
 
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