ID   GPMA1_BACTN             Reviewed;         249 AA.
AC   Q8A8R2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=BPG-dependent PGAM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=PGAM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=dPGM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN   Name=gpmA1 {ECO:0000255|HAMAP-Rule:MF_01039}; OrderedLocusNames=BT_1105;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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; AE015928; AAO76212.1; -; Genomic_DNA.
DR   RefSeq; NP_810018.1; NC_004663.1.
DR   RefSeq; WP_004295282.1; NZ_UYXG01000015.1.
DR   AlphaFoldDB; Q8A8R2; -.
DR   SMR; Q8A8R2; -.
DR   STRING; 226186.BT_1105; -.
DR   PaxDb; Q8A8R2; -.
DR   PRIDE; Q8A8R2; -.
DR   EnsemblBacteria; AAO76212; AAO76212; BT_1105.
DR   GeneID; 66749448; -.
DR   KEGG; bth:BT_1105; -.
DR   PATRIC; fig|226186.12.peg.1129; -.
DR   eggNOG; COG0588; Bacteria.
DR   HOGENOM; CLU_033323_1_1_10; -.
DR   InParanoid; Q8A8R2; -.
DR   OMA; TEWNVAR; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001414; 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..249
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase 1"
FT                   /id="PRO_0000179846"
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"
SQ   SEQUENCE   249 AA;  28420 MW;  A4B8AE020DF031AB CRC64;
     MKRIVLLRHG ESLWNKENRF TGWTDVDLSE KGVEEACKAG DALREAGFSF EAAYTSYLKR
     AVKTLNCVLD RLDKDWIPVE KTWRLNEKHY GMLQGLNKSE TAVQYGEEQV HIWRRSYDVA
     PAPVGKDDPR NPGMDIRYAG VPDSELPRTE SLKDTIGRVM PYWKCIIFPA LMYKDSLLVV
     AHGNSLRGII KHLKGISDTD ISNLNLPTAV PYVFEFDDRL VLVKDYYLGN PEEIRKRAEA
     VAKQGMAKK