GPMI_METH1
ID GPMI_METH1 Reviewed; 499 AA.
AC Q6Y8Q8; D1J8G9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgm;
GN OrderedLocusNames=MHO_3810;
OS Metamycoplasma hominis (strain ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC
OS 10111 / PG21) (Mycoplasma hominis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=347256;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Raherison S., Gonzalez P., Charron A., Renaudin H., Bebear C., Bebear C.M.;
RT "Identification of two multidrug efflux pump genes associated with
RT ciprofloxacin and ethidium bromide resistance in Mycoplasma hominis.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC 10111 / PG21;
RX PubMed=19816563; DOI=10.1371/journal.pgen.1000677;
RA Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A.,
RA Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A.,
RA Bebear C.;
RT "Life on arginine for Mycoplasma hominis: clues from its minimal genome and
RT comparison with other human urogenital mycoplasmas.";
RL PLoS Genet. 5:E1000677-E1000677(2009).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01038};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01038}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000255|HAMAP-Rule:MF_01038}.
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DR EMBL; AY169817; AAO39423.1; -; Genomic_DNA.
DR EMBL; FP236530; CAX37516.1; -; Genomic_DNA.
DR RefSeq; WP_012855655.1; NC_013511.1.
DR AlphaFoldDB; Q6Y8Q8; -.
DR SMR; Q6Y8Q8; -.
DR STRING; 347256.MHO_3810; -.
DR PRIDE; Q6Y8Q8; -.
DR EnsemblBacteria; CAX37516; CAX37516; MHO_3810.
DR KEGG; mho:MHO_3810; -.
DR eggNOG; COG0696; Bacteria.
DR HOGENOM; CLU_026099_2_0_14; -.
DR OMA; FMDGRDT; -.
DR OrthoDB; 338375at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002631; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..499
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212168"
FT ACT_SITE 60
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 253..256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 391
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 395
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 434
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 435
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ SEQUENCE 499 AA; 56245 MW; E0A99E5D4BA72B1A CRC64;
MKKIILTIID GLGLRKERQG NAYLQAKHPC FDYLFSMCPN SVLQASGQYV GLPEGQIGNS
EVGHLNIGAG RVVYTGLSLI NKAIENNTFK DNEILNDVID KTIKNNTTLH VMGLLSNGGV
HSLDLHLFEI LKLAHSKGLK NVSVHVFGDG RDVKPQSIKN SLETLKDLCQ KFGYKISSIS
GRFYAMDRDS IFSRNQEAYD AILGQSKNVI ENIDDYIESQ YKKGIFDEFF EPAQLKDGVF
VKNGDSIIFF NFRPDRARQL SHMFIGSNLY TYKPKNQVQI DNFVSLMKYE GINSKIAFKE
MEVVNPLGKV LESNDIKQLR LAETQKYAHV TFFFDGGVDI EYKNENRILV DSLKVDSFAD
YPHMSAKEIT DSLLNNIEKN DFIIMNYANP DMVGHTGNLN ATIEAIEFLD SQFQRILEYV
SLNHENVTWF ITADHGNAEI TEDENNKPAT KHTTSPVMFI CTDKNVNLGN GSLCDVAPTI
LDYLKINKPK EMTGKSLLK
