ID H6MZW7_GORPV Unreviewed; 295 AA.
AC H6MZW7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN OrderedLocusNames=GPOL_c21860 {ECO:0000313|EMBL:AFA73218.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73218.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA73218.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC EC=5.1.3.15; Evidence={ECO:0000256|ARBA:ARBA00001096};
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC {ECO:0000256|ARBA:ARBA00005866, ECO:0000256|PIRNR:PIRNR016020}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003119; AFA73218.1; -; Genomic_DNA.
DR RefSeq; WP_014359872.1; NC_016906.1.
DR AlphaFoldDB; H6MZW7; -.
DR STRING; 1112204.GPOL_c21860; -.
DR KEGG; gpo:GPOL_c21860; -.
DR eggNOG; COG0676; Bacteria.
DR HOGENOM; CLU_048345_4_0_11; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09020; D-hex-6-P-epi_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR025532; G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR PANTHER; PTHR11122; APOSPORY-ASSOCIATED PROTEIN C-RELATED; 1.
DR PANTHER; PTHR11122:SF39; GLUCOSE-6-PHOSPHATE 1-EPIMERASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PIRNR:PIRNR016020};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 295 AA; 31452 MW; EBC87EC091C712D5 CRC64;
MTTSGDDATQ QFHGVRRGTV HGLDAHLIET PHAQAAISVF GGQVVSFRPF GSAHDAVWVS
PVLADLPTPI RGGIPVCWPY FAREGQTGDV PSHGYARTAR WAITGAVVTE TGEVEISLAP
EGLDQLELRL SMTVRVGATL EQGIHTHNPG TAPARLTEAL HNYFRVSDVA DVRVEGLAGL
TYADKFDGGA IHPQHGEWTL PSYPARSDRL YPGAGGTYRI VDPGFGRVIE IRGRQARTAV
VWNPGADVAA GMADVGPHWR EFVCVETANA GPDVVEVPAG ATHSMWQTIS VTPVS
//
