ID   GPMA1_NITMU             Reviewed;         237 AA.
AC   Q2YBZ1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Nmul_A0422;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB73730.1; -; Genomic_DNA.
DR   RefSeq; WP_011379784.1; NZ_FNVK01000001.1.
DR   AlphaFoldDB; Q2YBZ1; -.
DR   SMR; Q2YBZ1; -.
DR   STRING; 323848.Nmul_A0422; -.
DR   EnsemblBacteria; ABB73730; ABB73730; Nmul_A0422.
DR   KEGG; nmu:Nmul_A0422; -.
DR   eggNOG; COG0588; Bacteria.
DR   HOGENOM; CLU_033323_1_1_4; -.
DR   OMA; PWAAIRK; -.
DR   OrthoDB; 1122642at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002718; 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; 2.
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..237
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase 1"
FT                   /id="PRO_0000229131"
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   SITE            182
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ   SEQUENCE   237 AA;  26694 MW;  9527D9BEF69DB0F1 CRC64;
     MTQLVLLRHG ESVSNRDGCF TGWGDAPLTP RGEREAEQAG NLLKKAGHKF DICFTSELSR
     ANDTLRIVLS VMGQDEPVVQ RNWRLNERHY GALEGINRWK AIRKYGFCPI LSSQCRFDAP
     PPPLDPADIR FPGNQACYAT IDPGELPLGE SMRQAFARML PYWQQTITPE IQRGKRVLIV
     AHKHILRGLI MQLDGLSIIQ LIKLSVATGR PLIYELDDNL HPIRHYYADT GLTGHTG