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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   22-JUL-2015, entry version 45.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE            Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN   Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   OrderedLocusNames=Svir_02670 {ECO:0000313|EMBL:ACU95349.1};
OS   Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 /
OS   NBRC 12207 / P101).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharomonospora.
OX   NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU95349.1, ECO:0000313|Proteomes:UP000000841};
RN   [1] {ECO:0000313|EMBL:ACU95349.1, ECO:0000313|Proteomes:UP000000841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC   {ECO:0000313|Proteomes:UP000000841};
RX   PubMed=21304650;
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., Goker 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. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC       {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512,
CC       ECO:0000256|SAAS:SAAS00055510}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_01039, ECO:0000256|RuleBase:RU004512}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|HAMAP-Rule:MF_01039}.
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DR   EMBL; CP001683; ACU95349.1; -; Genomic_DNA.
DR   RefSeq; WP_012795782.1; NC_013159.1.
DR   ProteinModelPortal; C7MSY8; -.
DR   STRING; 471857.Svir_02670; -.
DR   EnsemblBacteria; ACU95349; ACU95349; Svir_02670.
DR   KEGG; svi:Svir_02670; -.
DR   PATRIC; 23390910; VBISacVir111818_0265.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; PIKRYYL; -.
DR   OrthoDB; EOG6C8N1H; -.
DR   BioCyc; SVIR471857:GHAV-267-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000841; Chromosome.
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 {ECO:0000313|Proteomes:UP000000841};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS00055541};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS00055497};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000841}.
FT   REGION       11     18       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       24     25       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       90     93       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      117    118       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      185    186       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   ACT_SITE     12     12       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE    184    184       {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   BINDING      63     63       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   BINDING     101    101       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
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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