ID GPMA_BORDL Reviewed; 250 AA.
AC B5RMK4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 36.
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=BDU_661;
OS Borrelia duttonii (strain Ly).
OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia.
OX NCBI_TaxID=412419;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ly;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia
RT duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(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; CP000976; ACH93590.1; -; Genomic_DNA.
DR RefSeq; YP_002222296.1; NC_011229.1.
DR ProteinModelPortal; B5RMK4; -.
DR STRING; 412419.BDU_661; -.
DR PRIDE; B5RMK4; -.
DR EnsemblBacteria; ACH93590; ACH93590; BDU_661.
DR GeneID; 6917887; -.
DR KEGG; bdu:BDU_661; -.
DR PATRIC; 20563438; VBIBorDut9941_0670.
DR eggNOG; COG0588; -.
DR HOGENOM; HOG000221682; -.
DR KO; K01834; -.
DR OMA; GQSDWNL; -.
DR ProtClustDB; PRK14115; -.
DR BioCyc; BDUT412419:GJ78-661-MONOMER; -.
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 1 250 2,3-bisphosphoglycerate-dependent
FT phosphoglycerate mutase.
FT /FTId=PRO_1000135922.
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 250 AA; 28598 MW; 096FECA5C4047ED4 CRC64;
MYKLVLVRHG ESEWNKENLF TGWTDVKLSE KGVSEACEGG RILKEEGYSF DIAFSSMLVR
ANDTLNIILC ELGQSYIDVE KSWRLNERHY GALQGLNKAE TAEKYGEDKV LIWRRSYNVP
PMPLDESDKR HPIHDSRYKN IPKSELPSTE CLKDTVARVI PYWTDKIAKA ILEGKRVIVA
AHGNSLRALV KYLDNMSEED ILKLNIPTGI PLVYELDKNL KPVKHYYLGD EDKIKAAMES
VANQGKKIDR
//
