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Database: UniProt
Entry: A0A317VGX2_9EURO
LinkDB: A0A317VGX2_9EURO
Original site: A0A317VGX2_9EURO 
ID   A0A317VGX2_9EURO        Unreviewed;       161 AA.
AC   A0A317VGX2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   13-SEP-2023, entry version 11.
DE   SubName: Full=Putative ribose/galactose isomerase {ECO:0000313|EMBL:PWY73614.1};
GN   ORFNames=BO70DRAFT_373107 {ECO:0000313|EMBL:PWY73614.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY73614.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY73614.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY73614.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC       {ECO:0000256|ARBA:ARBA00008754}.
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:PWY73614.1}.
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DR   EMBL; MSFL01000024; PWY73614.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VGX2; -.
DR   STRING; 1448321.A0A317VGX2; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_373107; -.
DR   OrthoDB; 1472732at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR   InterPro; IPR011860; Rib-5-P_Isoase_Actino.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   NCBIfam; TIGR02133; RPI_actino; 1.
DR   NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR   PANTHER; PTHR43732:SF1; RIBOSE 5-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR43732; RIBOSE 5-PHOSPHATE ISOMERASE-RELATED; 1.
DR   Pfam; PF02502; LacAB_rpiB; 1.
DR   PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PWY73614.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
SQ   SEQUENCE   161 AA;  17224 MW;  5A1536BF12AA3639 CRC64;
     MSDTKPIRIV MACDEAGQPY KEILKAALEK NPLVESVQDV GVNSTSDKTA YPHPAVAGAR
     LIKEGQADRG LFICGTGLGV AISANKVPGI RAVTAHDSFS VERSILSNDA QVLCFGQRVI
     GIELAKKLAN EWVTYRFDPK SASAAKVQAI SDYEKEFATA V
//
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