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Database: UniProt
Entry: A9BUH9_DELAS
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Original site: A9BUH9_DELAS 
ID   A9BUH9_DELAS            Unreviewed;       213 AA.
AC   A9BUH9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABX33882.1};
GN   OrderedLocusNames=Daci_1238 {ECO:0000313|EMBL:ABX33882.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX33882.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX33882.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000884; ABX33882.1; -; Genomic_DNA.
DR   RefSeq; WP_012203168.1; NC_010002.1.
DR   AlphaFoldDB; A9BUH9; -.
DR   STRING; 398578.Daci_1238; -.
DR   GeneID; 24117481; -.
DR   KEGG; dac:Daci_1238; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_9_5_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR48100:SF34; BROAD-SPECIFICITY PHOSPHATASE YOR283W; 1.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT   ACT_SITE        11
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        84
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         10..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   213 AA;  23053 MW;  EC69248F8E7DC52E CRC64;
     MQATRIIAIR HGETAWNVDA RIQGHLDIPL NDMGLWQAAQ AGKALAGEPV AAIYSSDLLR
     AYVTAEAVAA STGATLTADK GLRERCFGRF EGQTFNDIEA SHPEDALRWR KRDPEFVPAG
     GGESLLMLRD RISATVNRLA SGHPGEQIVI VAHGGVMDVL YRLATHQEVQ APRTWALGNA
     AINRLLWTPQ GLGLVGWGDV QHLEGGARDE VFS
//
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