ID GPMA_PORG3 Reviewed; 248 AA.
AC B2RHB7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE Short=BPG-dependent PGAM;
DE Short=PGAM;
DE Short=Phosphoglyceromutase;
DE Short=dPGM;
DE EC=5.4.2.1;
GN Name=gpmA; OrderedLocusNames=PGN_0243;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Porphyromonadaceae; Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / JCM 12257;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis
RT strain ATCC 33277 and genomic comparison with strain W83 revealed
RT extensive genome rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC 3-phosphoglycerate (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily.
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DR EMBL; AP009380; BAG32762.1; -; Genomic_DNA.
DR RefSeq; YP_001928359.1; NC_010729.1.
DR ProteinModelPortal; B2RHB7; -.
DR SMR; B2RHB7; 3-234.
DR STRING; 431947.PGN_0243; -.
DR EnsemblBacteria; BAG32762; BAG32762; PGN_0243.
DR GeneID; 6330060; -.
DR KEGG; pgn:PGN_0243; -.
DR PATRIC; 22973420; VBIPorGin26334_0241.
DR eggNOG; COG0588; -.
DR HOGENOM; HOG000221682; -.
DR KO; K01834; -.
DR OMA; GQSDWNL; -.
DR ProtClustDB; PRK14115; -.
DR UniPathway; UPA00109; UER00186.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:HAMAP.
DR GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR HAMAP; MF_01039; PGAM_GpmA; 1; -.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycolysis; Isomerase.
FT CHAIN 1 248 2,3-bisphosphoglycerate-dependent
FT phosphoglycerate mutase.
FT /FTId=PRO_1000135964.
FT ACT_SITE 9 9 Tele-phosphohistidine intermediate (By
FT similarity).
FT ACT_SITE 182 182 By similarity.
FT SITE 60 60 Interaction with carboxyl group of
FT phosphoglycerates (By similarity).
SQ SEQUENCE 248 AA; 28737 MW; 59B9222CA897A18B CRC64;
MKRIVLIRHG ESLWNKENRF TGWTDVDLSE KGIEEAKKAG ELMKKEGFQF TKAYTSYLKR
AVKTLNGVLD VMDLDWIPVE KTWRLNEKHY GMLQGLNKAE TAEKYGDEQV LIWRRSYDVP
PTPMEKEDPR SPFMDPRYKG VCEKDLPLTE ALCDTVNRIL PYWNETIFPT LKEHDEVLVA
AHGNSLRGII KVLKNISDED IISLNLPTAV PYVFEFDDNL RLVKDYFLGD PEEIKKLMEA
VANQGKKK
//
