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GPMA_HAEIE
ID   GPMA_HAEIE              Reviewed;         227 AA.
AC   A5UDW8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, 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};
GN   OrderedLocusNames=CGSHiEE_08310;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98969.1; -; Genomic_DNA.
DR   RefSeq; WP_005652337.1; NC_009566.1.
DR   AlphaFoldDB; A5UDW8; -.
DR   SMR; A5UDW8; -.
DR   KEGG; hip:CGSHiEE_08310; -.
DR   HOGENOM; CLU_033323_1_5_6; -.
DR   OMA; RMLPYWY; -.
DR   UniPathway; UPA00109; UER00186.
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   3: Inferred from homology;
KW   Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..227
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000064062"
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"
SQ   SEQUENCE   227 AA;  26019 MW;  37E56B1BCDE72F7B CRC64;
     MELVFIRHGF SEWNAKNLFT GWRDVNLTER GVEEAKAAGK KLLDKGYEFD IAFTSVLTRA
     IKTCNIVLEE SHQLWIPQVK NWRLNERHYG ALQGLDKKAT AEQYGDEQVH IWRRSYDISP
     PDLDPQDPNS AHNDRRYANI PSDVVPNAEN LKLTLERALP FWEDQIAPAM LSGKRVLVVA
     HGNSLRALAK HIIGISDAEI MDFEIPTGQP LVLKLDDKLN YVEHYYL
 
 
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