GPMA2_GLOVI
ID GPMA2_GLOVI Reviewed; 219 AA.
AC Q7NJF7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=PGAM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=dPGM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN Name=gpmA2 {ECO:0000255|HAMAP-Rule:MF_01039}; OrderedLocusNames=gll1875;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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 -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; BA000045; BAC89816.1; -; Genomic_DNA.
DR RefSeq; NP_924821.1; NC_005125.1.
DR RefSeq; WP_011141873.1; NC_005125.1.
DR AlphaFoldDB; Q7NJF7; -.
DR SMR; Q7NJF7; -.
DR STRING; 251221.35212441; -.
DR EnsemblBacteria; BAC89816; BAC89816; BAC89816.
DR KEGG; gvi:gll1875; -.
DR PATRIC; fig|251221.4.peg.1907; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_4_3; -.
DR InParanoid; Q7NJF7; -.
DR OrthoDB; 1122642at2; -.
DR PhylomeDB; Q7NJF7; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000557; 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; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..219
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase 2"
FT /id="PRO_0000179880"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 85
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 112..113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 156..157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 155
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 219 AA; 24664 MW; C5FEA80461A5F5DC CRC64;
MALLVMVRHG QSIWNLENRF TGWTDVPLTE KGRAEARACG ELIYCVPFAV AFTSKLTRAQ
DTLRLILEAA DQPDVPVIED QALNERHYGE LQGLNKAETA AKYGEETVRQ WRRSLEGRPP
GGESLKDTAL RSLRYFYEKI VPELEAGKNV LVSAHGNTIR AILMELDHLS PEQVEKVEIE
YCVPVAFEHQ ADGTFSQVLM PRCDIIRPPQ PPARSIARL
