GPMA_BORBU
ID GPMA_BORBU Reviewed; 248 AA.
AC O51602;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
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=BB_0658;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of a phosphoglycerate mutase gpmA from Borrelia
RT burgdorferi B31.";
RL Submitted (APR-2012) to the PDB data bank.
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; AE000783; AAC67007.2; -; Genomic_DNA.
DR PIR; A70182; A70182.
DR RefSeq; NP_212792.2; NC_001318.1.
DR RefSeq; WP_002657375.1; NC_001318.1.
DR PDB; 4EMB; X-ray; 2.30 A; A/B/C/D=1-248.
DR PDBsum; 4EMB; -.
DR AlphaFoldDB; O51602; -.
DR SMR; O51602; -.
DR STRING; 224326.BB_0658; -.
DR PRIDE; O51602; -.
DR EnsemblBacteria; AAC67007; AAC67007; BB_0658.
DR GeneID; 56567468; -.
DR KEGG; bbu:BB_0658; -.
DR PATRIC; fig|224326.49.peg.1049; -.
DR HOGENOM; CLU_033323_1_1_12; -.
DR OMA; RMLPYWY; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
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; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..248
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000179852"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 87
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 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4EMB"
FT TURN 13..18
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:4EMB"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:4EMB"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4EMB"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:4EMB"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4EMB"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4EMB"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:4EMB"
SQ SEQUENCE 248 AA; 28379 MW; 213845B5ACD16DCB CRC64;
MYKLVLVRHG ESEWNKENLF TGWTDVKLSD KGIDEAVEAG LLLKQEGYSF DIAFSSLLSR
ANDTLNIILR ELGQSYISVK KTWRLNERHY GALQGLNKSE TAAKYGEDKV LIWRRSYDVP
PMSLDESDDR HPIKDPRYKH IPKRELPSTE CLKDTVARVI PYWTDEIAKE VLEGKKVIVA
AHGNSLRALV KYFDNLSEED VLKLNIPTGI PLVYELDKDL NPIKHYYLGD ESKIKKAMES
VASQGKLK
