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Entry: A8LZG5_SALAI
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ID   A8LZG5_SALAI            Unreviewed;       255 AA.
AC   A8LZG5;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   11-JUN-2014, entry version 44.
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=5.4.2.11;
GN   Name=gpmA; OrderedLocusNames=Sare_0402;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micromonosporineae; Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S.,
RA   Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000850; ABV96331.1; -; Genomic_DNA.
DR   RefSeq; YP_001535322.1; NC_009953.1.
DR   ProteinModelPortal; A8LZG5; -.
DR   SMR; A8LZG5; 10-243.
DR   STRING; 391037.Sare_0402; -.
DR   EnsemblBacteria; ABV96331; ABV96331; Sare_0402.
DR   GeneID; 5703795; -.
DR   KEGG; saq:Sare_0402; -.
DR   PATRIC; 23429239; VBISalAre38676_0409.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; KDDERFP; -.
DR   OrthoDB; EOG6C8N1H; -.
DR   BioCyc; SARE391037:GH66-411-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
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   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Isomerase.
FT   REGION       29     30       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION       95     98       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION      122    123       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   ACT_SITE     17     17       Tele-phosphohistidine intermediate (By
FT                                similarity){EA2}.
FT   ACT_SITE    190    190       By similarity{EA2}.
FT   BINDING      23     23       2-phospho-D-glycerate (By
FT                                similarity){EA2}.
FT   BINDING      68     68       2-phospho-D-glycerate (By
FT                                similarity){EA2}.
FT   BINDING     106    106       2-phospho-D-glycerate (By
FT                                similarity){EA2}.
FT   BINDING     192    192       2-phospho-D-glycerate (By
FT                                similarity){EA2}.
SQ   SEQUENCE   255 AA;  28771 MW;  FE9B06E513DF3FCC CRC64;
     MTASEGPTVG TLVLLRHGES DWNAKNLFTG WVDVDLTGKG ETEARRGGEL LREHNLLPDV
     VHTSLLRRAI RTAELALETA ERNWIAVRRS WRLNERHYGA LQGKNKKQTL DEYGEEQFML
     WRRSYDTPPP PIADDDEWSQ VGDPRYRLLP TELMPRTECL KDVVERMLPY WYDSIVPDIL
     AGRTVLVAAH GNSLRALVKH LDQISDEAIA KLNIPTGIPL RYDLDPQLRP MTLGGTYLDP
     TAARDAAAAV ANQGR
//
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