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Database: UniProt/TrEMBL
Entry: C7MSY8_SACVD
LinkDB: C7MSY8_SACVD
Original site: C7MSY8_SACVD 
ID   C7MSY8_SACVD            Unreviewed;       249 AA.
AC   C7MSY8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   19-FEB-2014, entry version 31.
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=Svir_02670;
OS   Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 /
OS   NBRC 12207 / P101).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=471857;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101;
RX   DOI=10.4056/sigs.20263;
RA   Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA   Glavina del Rio T., Lucas S., Chen F., Tice H., Pitluck S.,
RA   Cheng J.-F., Chertkov O., Brettin T., Han C., Detter J.C., Kuske C.,
RA   Bruce D., Goodwin L., Chain P., D'haeseleer P., Chen A.,
RA   Palaniappan K., Ivanova N., Mavromatis K., Mikhailova N., Rohde M.,
RA   Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Saccharomonospora viridis type strain
RT   (P101).";
RL   Stand. Genomic Sci. 1:141-149(2009).
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; CP001683; ACU95349.1; -; Genomic_DNA.
DR   RefSeq; YP_003132176.1; NC_013159.1.
DR   ProteinModelPortal; C7MSY8; -.
DR   STRING; 471857.Svir_02670; -.
DR   EnsemblBacteria; ACU95349; ACU95349; Svir_02670.
DR   GeneID; 8385605; -.
DR   KEGG; svi:Svir_02670; -.
DR   PATRIC; 23390910; VBISacVir111818_0265.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; SYYLGDQ; -.
DR   OrthoDB; EOG6C8N1H; -.
DR   ProtClustDB; CLSK2536836; -.
DR   BioCyc; SVIR471857:GHAV-267-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:glycolysis; IEA:UniProtKB-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   REGION       24     25       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION       90     93       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION      117    118       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   ACT_SITE     12     12       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    184    184       By similarity.
FT   BINDING      18     18       2-phospho-D-glycerate (By similarity).
FT   BINDING      63     63       2-phospho-D-glycerate (By similarity).
FT   BINDING     101    101       2-phospho-D-glycerate (By similarity).
FT   BINDING     186    186       2-phospho-D-glycerate (By similarity).
SQ   SEQUENCE   249 AA;  27566 MW;  E875F3CE2A1917E3 CRC64;
     MAELGTLVLL RHGQSTWNAE NLFTGWVDVP LSEQGEAEAR RGGELLAEAG LLPDVVHTSL
     LRRAISTANI ALDVADRHWI DVRRDWRLNE RHYGALQGKN KKETLEQFGE EQFMLWRRSY
     DTPPPPIEPG SQYSQDGDVR YADLGDKLPT TECLKDVVER LLPYWESAIV PDLRAGKTVL
     IAAHGNSLRA LVKHLDGISD EDIVGLNIPT GIPLRYDLDE NLKPTNPGGT YLDPEAAEKA
     AAAVASQGR
//
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