ID GPMI_MYCPN Reviewed; 508 AA. AC P75167; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 134. 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=MPN_628; ORFNames=MP214; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; Evidence={ECO:0000255|HAMAP- CC 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 -!- INTERACTION: CC P75167; P04004: VTN; Xeno; NbExp=2; IntAct=EBI-2259565, EBI-1036653; CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. {ECO:0000255|HAMAP-Rule:MF_01038}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00089; AAB95862.1; -; Genomic_DNA. DR PIR; S73540; S73540. DR RefSeq; NP_110317.1; NC_000912.1. DR RefSeq; WP_010874985.1; NZ_OU342337.1. DR AlphaFoldDB; P75167; -. DR SMR; P75167; -. DR IntAct; P75167; 6. DR STRING; 272634.MPN_628; -. DR EnsemblBacteria; AAB95862; AAB95862; MPN_628. DR KEGG; mpn:MPN_628; -. DR PATRIC; fig|272634.6.peg.692; -. DR HOGENOM; CLU_026099_2_0_14; -. DR OrthoDB; 9800863at2; -. DR BioCyc; MetaCyc:MONOMER-550; -. DR BioCyc; MPNE272634:G1GJ3-1009-MONOMER; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016020; C:membrane; IDA:AgBase. 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 GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:AgBase. DR CDD; cd16010; iPGM; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 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 NCBIfam; TIGR01307; pgm_bpd_ind; 1. DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1. DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1. DR Pfam; PF06415; iPGM_N; 1. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001492; IPGAM; 1. DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. PE 1: Evidence at protein level; KW Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome. FT CHAIN 1..508 FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate FT mutase" FT /id="PRO_0000212175" FT ACT_SITE 61 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 11 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 61 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 150..151 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 257..260 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 332 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 397 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 401 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 438 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 439 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 456 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" SQ SEQUENCE 508 AA; 56375 MW; A856375375B09F5E CRC64; MHKKVLLAIL DGYGISNKQH GNAVYHAKTP ALDSLIKDYP CVMLEASGEA VGLPQGQIGN SEVGHLNIGA GRIVYTGLSL INQNIKTGAF HHNQVLLEAI ARAKANNAKL HLIGLFSHGG VHSHMDHLYA LIKLAAPQVK MVLHLFGDGR DVAPCTMKSD LEAFMVFLKD YHNVIIGTLG GRYYGMDRDQ RWDREEIAYN AILGNSKASF TDPVAYVQSA YDQKVTDEFL YPAVNGNVDK EQFALKDHDS VIFFNFRPDR ARQMSHMLFQ TDYYDYTPKA GRKYNLFFVT MMNYEGIKPS AVVFPPETIP NTFGEVIAHN KLKQLRIAET EKYAHVTFFF DGGVEVDLPN ETKCMVPSLK VATYDLAPEM ACKGITDQLL NQINQFDLTV LNFANPDMVG HTGNYAACVQ GLEALDVQIQ RIIDFCKANH ITLFLTADHG NAEEMIDSNN NPVTKHTVNK VPFVCTDTNI DLQQDSASLA NIAPTILAYL GLKQPAEMTA NSLLISKK //