(data stored in ACNUC7421 zone)

SWISSPROT: GPMI_PSEHT

ID   GPMI_PSEHT              Reviewed;         514 AA.
AC   Q3IIE4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 82.
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=gpmM;
GN   OrderedLocusNames=PSHAa0366;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC       {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; CR954246; CAI85464.1; -; Genomic_DNA.
DR   RefSeq; WP_011327077.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIE4; -.
DR   SMR; Q3IIE4; -.
DR   STRING; 326442.PSHAa0366; -.
DR   EnsemblBacteria; CAI85464; CAI85464; PSHAa0366.
DR   KEGG; pha:PSHAa0366; -.
DR   PATRIC; fig|326442.8.peg.349; -.
DR   eggNOG; ENOG4105CJI; Bacteria.
DR   eggNOG; COG0696; LUCA.
DR   HOGENOM; HOG000223664; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   OrthoDB; POG091H01EL; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16010; iPGM; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   HAMAP; MF_01038; GpmI; 1.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 1.
DR   SUPFAM; SSF53649; SSF53649; 2.
DR   SUPFAM; SSF64158; SSF64158; 1.
DR   TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IIE4.
DR   SWISS-2DPAGE; Q3IIE4.
KW   Complete proteome; Glycolysis; Isomerase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    514       2,3-bisphosphoglycerate-independent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000212187.
FT   REGION      155    156       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   REGION      263    266       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   ACT_SITE     64     64       Phosphoserine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01038}.
FT   METAL        14     14       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   METAL        64     64       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   METAL       404    404       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   METAL       408    408       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   METAL       445    445       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   METAL       446    446       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   METAL       464    464       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   BINDING     125    125       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   BINDING     187    187       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   BINDING     193    193       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
FT   BINDING     337    337       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01038}.
SQ   SEQUENCE   514 AA;  55865 MW;  56E255BF94164196 CRC64;
     MSEHKKPLVL MILDGWGYRE DEQSNAILAA NTPVLDELWA TRPRTLISAS GFDVGLPDGQ
     MGNSEVGHVN LGAGRVVYQD FTRITKAIND GEFDSTPALV DNIDKAVSAD KAVHIMGLLS
     PGGVHSHEDH IVASIELAAK RGAKEVYFHG FLDGRDTPPR SAKASIERIE AVFAKLQCGR
     LASLIGRYYA MDRDNRWNRV EKAYNLLTLA QGDFSYPTGV SALEAAYERD ENDEFVAAST
     ITPAGAEPVQ INDGDTVIFA NFRADRAREI TRAFVEPNFD GFAKQKSPAL SAFVMMTEYA
     ADIDAPVAFG PTPLVNVLGE WFEKHGKTQL RISETEKYAH VTFFFSGGRE DEFNGETREL
     IPSPQVATYD LQPEMNSEML TDKLVAAIKS GKYDAIICNY PNGDMVGHSG VFAAAVKACE
     AVDHCIGRVV AALNKYGGEA LITADHGNAE QMANLKTGQA HTAHTSEPVP FIYVGRDATA
     SEGKALSDVA PTMLHLMGME QPTEMTGKPI MTLK
//

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