ID   GPMI_RHOBA              Reviewed;         543 AA.
AC   Q7UFG7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=RB8562;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01038}.
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DR   EMBL; BX294147; CAD78715.1; -; Genomic_DNA.
DR   RefSeq; NP_868437.1; NC_005027.1.
DR   RefSeq; WP_011121922.1; NC_005027.1.
DR   AlphaFoldDB; Q7UFG7; -.
DR   SMR; Q7UFG7; -.
DR   STRING; 243090.RB8562; -.
DR   EnsemblBacteria; CAD78715; CAD78715; RB8562.
DR   KEGG; rba:RB8562; -.
DR   PATRIC; fig|243090.15.peg.4115; -.
DR   eggNOG; COG0696; Bacteria.
DR   HOGENOM; CLU_026099_2_0_0; -.
DR   InParanoid; Q7UFG7; -.
DR   OrthoDB; 9800863at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
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; 3.40.720.10; 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   3: Inferred from homology;
KW   Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..543
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000212195"
FT   ACT_SITE        73
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         20
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         73
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         166..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         278..281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         428
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         432
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         469
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         470
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ   SEQUENCE   543 AA;  59011 MW;  D2AB2967D098CC45 CRC64;
     MVLTFMTATR RRPVVLIVRD GWGQNPDPKW NESNAVHLAN TPVDDKLTQE YPSVLIHTSG
     EDVGLPAGVM GNSEVGHQNI GAGRIVDQEV MRITRAIRDD SFFSNPVVTG AIDHVKKSGG
     RLHLLGLMSD GRVHSDLQHG IAVIDLAKRN GLTGDQLAIH AITDGRDTSP RGGLKFVSQL
     TDHCEASGVG VVASVIGRFY AMDRDLRWER VEAAYNLMTQ GTGQTFPSAS AAIESYYANP
     TESSRDGDEF ITASSIVPEG GSPITVQPGD AVLFMNYRGD RTREITKAFT FDDAAWKDIP
     GGGFDRGKKI DNLYFATMTG YETGLPVKVI FEKPAKMPNI LGEYVASKGL HQFRCAETEK
     YPHVTFFFND YRDNPFEEEE WGMAPSPRDV STYDQKPEMS AEDITEKVLK QIKSGKCDMI
     IVNYANGDMV GHTGVLEAAI KAVEKVDACV GRVVDATLAA GGSLVVTADH GNCEQMIDPE
     TGGPHTAHTT YQVPLIVVDP EFVGKPLREG GRLADIAPTV LALMGLEVPP EMTGRPLMET
     QTA
//