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GPMI_RHOPA
ID   GPMI_RHOPA              Reviewed;         504 AA.
AC   Q6NCX7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=pgm1;
GN   OrderedLocusNames=RPA0340;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572594; CAE25784.1; -; Genomic_DNA.
DR   RefSeq; WP_011155908.1; NC_005296.1.
DR   AlphaFoldDB; Q6NCX7; -.
DR   SMR; Q6NCX7; -.
DR   STRING; 258594.RPA0340; -.
DR   PRIDE; Q6NCX7; -.
DR   EnsemblBacteria; CAE25784; CAE25784; RPA0340.
DR   GeneID; 66891351; -.
DR   KEGG; rpa:RPA0340; -.
DR   eggNOG; COG0696; Bacteria.
DR   HOGENOM; CLU_026099_2_0_5; -.
DR   OMA; FMDGRDT; -.
DR   PhylomeDB; Q6NCX7; -.
DR   BioCyc; RPAL258594:TX73_RS01760-MON; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001426; 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..504
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000212196"
FT   ACT_SITE        63
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         63
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         153..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         254..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         330
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         457
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ   SEQUENCE   504 AA;  53352 MW;  C942A36F4E86F8CC CRC64;
     MQSRRPVMLV ILDGWGWRED PADNAVLQAK TPTFDALWTN GPHAFLRTSG KSVGLPNGQM
     GNSEVGHLNI GAGRVVMQDL PRISDAIANG EIERAPGLVA FIDKLKASGG TCHLMGLVSP
     GGVHSLQDHA CALAKILAKA GVKTVLHAFT DGRDTPPKSA VDDIVRLRAE LPPNVPIATV
     SGRYYAMDRD NRWERVSKAY GVIADADGPR FADANAVIAD GYAAGVNDEF IVPAVIGDYQ
     GMRDGDGVLC FNFRADRVRE ILAALLDSAF AGFPRKQVKQ IAAAAGMTQY STALDALMGT
     IFPPQSLVNG LGQVVADAGL HQLRMAETEK YPHVTYFLNG GEEVPYPGED RIMVPSPKVA
     TYDLQPEMSA PELGDKAVAA IESGKYDLIV LNFANPDMVG HTGSLPAAIK AVETVDTQLG
     HIVAAIRKAG GALLVTADHG NCEMMRDPET GGPHTAHTTN PVPVLLVGDN GPLADGQLSD
     LAPTLLKLME LPQPAEMTGK SLIG
 
 
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