(data stored in ACNUC7421 zone)

SWISSPROT: GPMI_LEGPC

ID   GPMI_LEGPC              Reviewed;         514 AA.
AC   A5IH96;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 79.
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}; OrderedLocusNames=LPC_2845;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000675; ABQ56746.1; -; Genomic_DNA.
DR   RefSeq; WP_011945657.1; NC_009494.2.
DR   SMR; A5IH96; -.
DR   EnsemblBacteria; ABQ56746; ABQ56746; LPC_2845.
DR   KEGG; lpc:LPC_2845; -.
DR   HOGENOM; HOG000223664; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   BioCyc; LPNE400673:LPC_RS02740-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
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;
DR   PRODOM; A5IH96.
DR   SWISS-2DPAGE; A5IH96.
KW   Glycolysis; Isomerase; Manganese; Metal-binding.
FT   CHAIN           1..514
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000063979"
FT   REGION          154..155
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   REGION          258..261
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   ACT_SITE        63
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           13
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           63
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           399
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           403
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           440
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           441
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           459
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         124
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         192
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         332
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ   SEQUENCE   514 AA;  57645 MW;  7E789E23003D5FA8 CRC64;
     MSHNAPLVLM ILDGWGYNEN DRYNAIAKAN TPQWDEWWQT CPHILLKASG LPVGLPDEQM
     GNSEVGHMHI GAGRVIQQDF TRINEAINNG KFAKNAVFHE VIDQLKKTEK SLHIMGLLSP
     GGVHSHEQHL FALLALCNQK KFRSVHLHLF LDGRDTPPQS ALDSLKCLNE ELVKHPVATI
     NSICGRYYAM DRDKRWERVE PVYNLLTQGK SEHQFPDAET AIHFYYKNKI SDEFVPPTLI
     GKEHSIQDGD AVLFFNFRAD RARQLTSTFL DPLFKGFERK TLPKLSYFVS MTQYDKNLIT
     TIAFPPVPLN NTLGEVLSSH GLSQLRIAET EKYAHVTFFF NGGCESVFTN EERIMVPSPQ
     VATYDLQPEM SAPELTKTLI AAINSRDYHV IICNYANADM VGHTGNFEAT VQAIECLDQC
     MHQVWQALKN NGGKLLITAD HGNAEEMFSE ATNQAHTAHT SEPVPFLYVG GGWHFTHAEG
     SLIDIAPSLL ALLGITPPPE MTGRILLEKN HAHV
//

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