ID C7MSY8_SACVD Unreviewed; 249 AA.
AC C7MSY8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 01-MAY-2013, entry version 26.
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=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; GQSDWNL; -.
DR ProtClustDB; CLSK2536836; -.
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 ACT_SITE 12 12 Tele-phosphohistidine intermediate (By
FT similarity).
FT ACT_SITE 184 184 By similarity.
FT SITE 63 63 Interaction with carboxyl group of
FT phosphoglycerates (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
//
