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Database: UniProt
Entry: T0XZV9_9BACT
LinkDB: T0XZV9_9BACT
Original site: T0XZV9_9BACT 
ID   T0XZV9_9BACT            Unreviewed;       144 AA.
AC   T0XZV9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000313|EMBL:EQD25267.1};
GN   ORFNames=D084_Lepto4C00201G0004 {ECO:0000313|EMBL:EQD25267.1};
OS   Leptospirillum sp. Group IV 'UBA BS'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1260983 {ECO:0000313|EMBL:EQD25267.1, ECO:0000313|Proteomes:UP000017751};
RN   [1] {ECO:0000313|EMBL:EQD25267.1, ECO:0000313|Proteomes:UP000017751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23645189; DOI=10.1128/AEM.00202-13;
RA   Goltsman D.S., Dasari M., Thomas B.C., Shah M.B., VerBerkmoes N.C.,
RA   Hettich R.L., Banfield J.F.;
RT   "New group in the Leptospirillum clade: cultivation-independent community
RT   genomics, proteomics, and transcriptomics of the new species
RT   "Leptospirillum group IV UBA BS".";
RL   Appl. Environ. Microbiol. 79:5384-5393(2013).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQD25267.1}.
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DR   EMBL; AURA01000201; EQD25267.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0XZV9; -.
DR   PATRIC; fig|1260983.3.peg.449; -.
DR   HOGENOM; CLU_1794134_0_0_0; -.
DR   Proteomes; UP000017751; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
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   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017751}.
FT   BINDING         9..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         36..37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         80..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            79
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   144 AA;  15954 MW;  B53D27A49FFE5E9C CRC64;
     MERSEALNER HYGDLQGLNK DETAKKYGAE QVHIWRRSYD VAPPGGESLK MTRDRVLPYV
     HATILPALLR GENCLVVAHG NSLRAMVMEL DRMTKEQVLE LNIPTATPIL YRLGIVSPEE
     GTVPGLPGLT VLEKKILDGP PSPC
//
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