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Database: UniProt/TrEMBL
Entry: A8LZG5_SALAI
LinkDB: A8LZG5_SALAI
Original site: A8LZG5_SALAI 
ID   A8LZG5_SALAI            Unreviewed;       255 AA.
AC   A8LZG5;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   22-JUL-2015, entry version 54.
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=Sare_0402 {ECO:0000313|EMBL:ABV96331.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV96331.1, ECO:0000313|Proteomes:UP000001153};
RN   [1] {ECO:0000313|EMBL:ABV96331.1, ECO:0000313|Proteomes:UP000001153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV96331.1,
RC   ECO:0000313|Proteomes:UP000001153};
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. {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; CP000850; ABV96331.1; -; Genomic_DNA.
DR   RefSeq; WP_012180605.1; 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; PIKRYYL; -.
DR   OrthoDB; EOG6C8N1H; -.
DR   BioCyc; SARE391037:GH66-411-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001153; 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:UP000001153};
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}.
FT   REGION       16     23       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       29     30       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       95     98       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      122    123       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      191    192       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   ACT_SITE     17     17       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE    190    190       {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   BINDING      68     68       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   BINDING     106    106       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
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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