ID U4K9Y5_9VIBR Unreviewed; 295 AA.
AC U4K9Y5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN ORFNames=VIBNI_A0839 {ECO:0000313|EMBL:CCO57007.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO57007.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO57007.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203526; CCO57007.1; -; Genomic_DNA.
DR RefSeq; WP_022550045.1; NC_022528.1.
DR AlphaFoldDB; U4K9Y5; -.
DR STRING; 28173.VIBNI_A0839; -.
DR KEGG; vni:VIBNI_A0839; -.
DR PATRIC; fig|1260221.3.peg.805; -.
DR eggNOG; COG0676; Bacteria.
DR OrthoDB; 9790727at2; -.
DR Proteomes; UP000016895; Chromosome 1.
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:UP000016895}.
FT REGION 276..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 295 AA; 32401 MW; CB49FA17CDC48FE3 CRC64;
MELRTLPALT VLSDNVSIVE KDNVKIVRVI HEKAEAGIAL HGGHVVSFKP SGQQDLIWMS
KEAKFDGKAA LRGGVPVCWP WFGRIAAPAH GFARSSQWDL VEHRENENGV IVSLGLKPNA
ETKAIWDFDF EAILNVEISD TLTITLDVKN TDNKAWTFSG ALHTYLNVGD ILNTETTGMG
AEYIDSLQDD KVCQGGEVLK LTDTIDRVYT QPEAQIRVSD SSFDRTIVIE NQGHNSAVLW
NPWKEGAEGM GDMQDDGYQT MLCVESTLHA PSIEEGKTLQ PGESHQLATT ISLAN
//
