ID A0A423X216_9PEZI Unreviewed; 279 AA.
AC A0A423X216;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
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=VMCG_02358 {ECO:0000313|EMBL:ROW09763.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW09763.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW09763.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW09763.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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}.
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:ROW09763.1}.
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DR EMBL; LKEA01000004; ROW09763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X216; -.
DR STRING; 356882.A0A423X216; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000283895; 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 InterPro; IPR037171; NagB/RpiA_transferase-like.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895}.
SQ SEQUENCE 279 AA; 29532 MW; F946D7C85A59EF78 CRC64;
MATTSTSALS AVEQAKLIES SKRAAAYEAV KEHMDLTYTD IGIGSGSTVI YVVEAIAALG
KDVTNKMSFF PTGEQSRELI RAAGLRVQYI QDLSDAQQLD VCFDGADEVD EELNLIKGGG
ACLFQEKLVV TKAKKFVCVA DFRKHSARLG TNWKKGIPIE VVSQATGHVL SELRKIGAIN
PVLRSGLPGK AGSIVTDNGN SLIDAPFAPL AMAKDLKGKD GENGIWTVEA LADRIIKIVG
VVEVGLFAGA NGFEVQSGAQ KPVAAYFGMA DGTVDIRKA
//