GPMA1_NITEU
ID GPMA1_NITEU Reviewed; 234 AA.
AC Q82XS4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=NE0178;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(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 -!- 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; AL954747; CAD84089.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82XS4; -.
DR SMR; Q82XS4; -.
DR STRING; 228410.NE0178; -.
DR EnsemblBacteria; CAD84089; CAD84089; NE0178.
DR KEGG; neu:NE0178; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_1_4; -.
DR OMA; PWAAIRK; -.
DR PhylomeDB; Q82XS4; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001416; 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..234
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase 1"
FT /id="PRO_0000179897"
FT ACT_SITE 15
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 93
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 14..21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 93..96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 234 AA; 26889 MW; 40D612055414EF38 CRC64;
MNEIQEPIRL VLLRHGQSIW NQDRHFTGWG DIVLSPQGEQ EALRAGHLLK QAGFTFDACF
CSELQRASDT LAIVQSVMGL NHLSTYRTWR LNERHYGALE GMRPWAAIRK FGIWSTMKSQ
IRFDAAPPLL MPDDPRAPVN QPRYAAVDRT QLPLAESMQQ TLERVRPLWQ ETILPEIRQG
KRLLIVSHQN LLKTLVMQLE GLTGAQIMRL SITTGHPLCY ELDHSLVPVK RYYL
