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Database: UniProt
Entry: A0A177WBM5_BATDL
LinkDB: A0A177WBM5_BATDL
Original site: A0A177WBM5_BATDL 
ID   A0A177WBM5_BATDL        Unreviewed;       231 AA.
AC   A0A177WBM5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Ribose-5-phosphate isomerase {ECO:0000256|ARBA:ARBA00019150};
DE            EC=5.3.1.6 {ECO:0000256|ARBA:ARBA00011959};
DE   AltName: Full=D-ribose-5-phosphate ketol-isomerase {ECO:0000256|ARBA:ARBA00032273};
DE   AltName: Full=Phosphoriboisomerase {ECO:0000256|ARBA:ARBA00029734};
GN   ORFNames=BDEG_21520 {ECO:0000313|EMBL:OAJ37507.1};
OS   Batrachochytrium dendrobatidis (strain JEL423).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ37507.1, ECO:0000313|Proteomes:UP000077115};
RN   [1] {ECO:0000313|EMBL:OAJ37507.1, ECO:0000313|Proteomes:UP000077115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL423 {ECO:0000313|EMBL:OAJ37507.1,
RC   ECO:0000313|Proteomes:UP000077115};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA   Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA   James T.;
RT   "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAJ37507.1, ECO:0000313|Proteomes:UP000077115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL423 {ECO:0000313|EMBL:OAJ37507.1,
RC   ECO:0000313|Proteomes:UP000077115};
RA   Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT   "Lineage-specific infection strategies underlie the spectrum of fungal
RT   disease in amphibians.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC         EC=5.3.1.6; Evidence={ECO:0000256|ARBA:ARBA00001713};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC       5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC       1/1. {ECO:0000256|ARBA:ARBA00004988}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000256|ARBA:ARBA00008088}.
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DR   EMBL; DS022300; OAJ37507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177WBM5; -.
DR   STRING; 403673.A0A177WBM5; -.
DR   VEuPathDB; FungiDB:BDEG_21520; -.
DR   eggNOG; KOG3075; Eukaryota.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000077115; Unassembled WGS sequence.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:InterPro.
DR   CDD; cd01398; RPI_A; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.1360; -; 1.
DR   HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR   InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR   NCBIfam; TIGR00021; rpiA; 1.
DR   PANTHER; PTHR11934; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11934:SF0; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF75445; D-ribose-5-phosphate isomerase (RpiA), lid domain; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OAJ37507.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077115}.
SQ   SEQUENCE   231 AA;  24659 MW;  25CB9AE6C8930E1D CRC64;
     MLEIAKQLAS FRAIDERVST STKVIGIGSG STIVYAVQRL AERFKQESLP IQACIATSFQ
     AQQLILEAGL PLGTLNQYPL IDVAFDGADE IDTSLNCIKG GGACHLQEKL VASNAKLFYL
     VADHRKDSKV LGTQWKQGVP IEVTPMVYVA VMQKIKTMGG KPTLRMAAKK AGPVVTDNGN
     FVIDADFGEI CDPAALNVQL IGVPGIVETG LFCNMVNGVY FGLPDGTVKA V
//
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