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2,3-bisphosphoglycerate-independent phosphoglycerate mutase (BPG-independent PGAM) (Phosphoglyceromutase) (iPGM) (EC 5.4.2.12)

 GPMI_MYCPN              Reviewed;         508 AA.
P75167;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-FEB-2018, entry version 114.
RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgm;
OrderedLocusNames=MPN_628; ORFNames=MP214;
Mycoplasma pneumoniae (strain ATCC 29342 / M129).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=272634;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
PubMed=8948633; DOI=10.1093/nar/24.22.4420;
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma
pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).
-!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
{ECO:0000255|HAMAP-Rule:MF_01038}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
Rule:MF_01038};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
Rule:MF_01038}.
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
-!- INTERACTION:
P04004:VTN (xeno); NbExp=2; IntAct=EBI-2259565, EBI-1036653;
-!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
family. {ECO:0000255|HAMAP-Rule:MF_01038}.
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EMBL; U00089; AAB95862.1; -; Genomic_DNA.
PIR; S73540; S73540.
RefSeq; NP_110317.1; NC_000912.1.
RefSeq; WP_010874985.1; NC_000912.1.
ProteinModelPortal; P75167; -.
SMR; P75167; -.
IntAct; P75167; 6.
EnsemblBacteria; AAB95862; AAB95862; MPN_628.
GeneID; 877355; -.
KEGG; mpn:MPN628; -.
PATRIC; fig|272634.6.peg.692; -.
KO; K15633; -.
OMA; FMDGRDT; -.
BioCyc; MetaCyc:MONOMER-550; -.
BioCyc; MPNE272634:G1GJ3-1009-MONOMER; -.
UniPathway; UPA00109; UER00186.
Proteomes; UP000000808; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
GO; GO:0052014; P:catabolism by symbiont of host protein; IDA:AgBase.
GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:AgBase.
CDD; cd16010; iPGM; 1.
Gene3D; 3.40.1450.10; -; 1.
Gene3D; 3.40.720.10; -; 2.
HAMAP; MF_01038; GpmI; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR011258; BPG-indep_PGM_N.
InterPro; IPR006124; Metalloenzyme.
InterPro; IPR036646; PGAM_B_sf.
InterPro; IPR005995; Pgm_bpd_ind.
PANTHER; PTHR31637; PTHR31637; 1.
Pfam; PF06415; iPGM_N; 1.
Pfam; PF01676; Metalloenzyme; 1.
PIRSF; PIRSF001492; IPGAM; 1.
SUPFAM; SSF53649; SSF53649; 2.
SUPFAM; SSF64158; SSF64158; 1.
TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
1: Evidence at protein level;
Complete proteome; Glycolysis; Isomerase; Manganese; Metal-binding;
Reference proteome.
CHAIN 1 508 2,3-bisphosphoglycerate-independent
phosphoglycerate mutase.
/FTId=PRO_0000212175.
REGION 150 151 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01038}.
REGION 257 260 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01038}.
ACT_SITE 61 61 Phosphoserine intermediate.
{ECO:0000255|HAMAP-Rule:MF_01038}.
METAL 11 11 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 61 61 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 397 397 Manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 401 401 Manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 438 438 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 439 439 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 456 456 Manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 122 122 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 182 182 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 188 188 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 332 332 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
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


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