ID A1SX88_PSYIN Unreviewed; 301 AA.
AC A1SX88;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=Ping_2366 {ECO:0000313|EMBL:ABM04103.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM04103.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM04103.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM04103.1,
RC ECO:0000313|Proteomes:UP000000639};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000510; ABM04103.1; -; Genomic_DNA.
DR RefSeq; WP_011770663.1; NC_008709.1.
DR AlphaFoldDB; A1SX88; -.
DR STRING; 357804.Ping_2366; -.
DR KEGG; pin:Ping_2366; -.
DR eggNOG; COG0676; Bacteria.
DR HOGENOM; CLU_048345_4_0_6; -.
DR OrthoDB; 9790727at2; -.
DR Proteomes; UP000000639; 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:UP000000639}.
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 301 AA; 33221 MW; 84650196CE7774F1 CRC64;
MLCHISLFKI KTLSTAISIQ ADAAGYEFLI IEHKKFNAAF ALHGGHLVHF QLKEQQPIIW
LSKTAIYNQQ KAIRGGVPVC WPWFGAADKS LGENLPAHGF ARTSKWELAA HNEFPEGVEI
ELRLTDSAAT RDIWPFQFEL LLKATLTDQI KLELISKNTG NIPFSYRGAL HSYLNISTPE
SCAISGLNNH YNDSLDNGLA KSGDSTLQIT GPIDAIYKKA LSPITLSDKQ FNRQLIIDNS
GNDAEVLWTP WIAGAKAFAD MPDQGYKTMF CIESAITNKS GVRVKPGHSH SLSTTIRSHT
G
//