ID A0A395MZL9_9HYPO Unreviewed; 909 AA.
AC A0A395MZL9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013920};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
DE AltName: Full=Pentose-5-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00030599};
DE AltName: Full=RPE {ECO:0000256|ARBA:ARBA00029933};
GN ORFNames=FIE12Z_2508 {ECO:0000313|EMBL:RFN53160.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN53160.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN53160.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN53160.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000256|ARBA:ARBA00001782};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage):
CC step 1/1. {ECO:0000256|ARBA:ARBA00005016}.
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541}.
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:RFN53160.1}.
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DR EMBL; PXXK01000049; RFN53160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MZL9; -.
DR STRING; 2594813.A0A395MZL9; -.
DR UniPathway; UPA00115; UER00411.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 412..537
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 751..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..896
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 101174 MW; E3A3ABA4A5EBEA4C CRC64;
MAPKTIIAPS ILSADFAQLG HDCARTMKQG ADWLHVDIMD GHFVPNITFG PPVVAAIRGH
VDQPTEAHGR GTFDCHMMIA EPKKWVKEFK KAGCNLYCFH YEAAFSSAAE NPEDQTDEKT
NPKALIRYIH DQGLLAGIAI KPDTSVDVLW EILENSEEKE RPDMVLVMTV YPGFGGQKFM
ASELPKVQAL REKYPELNIE VDGGIGPKTI DEAADAGANV IVAGSAVFGA NDPSEVIAQL
RQSVDARNAN SNPLSLAQPL SSNSIARVIM KRKAGAAAGA SKANKKKSKP SLGAEEAQKR
FRAGLFDQKV LNSYTEQYAQ SEPYKHAVIN GLVDDSLLRS VRSEIKANVE FTPKETDIYK
IHQSGDLANL DGLDDESLAK LPSLLKLRDA IYSESFRNYV SHITDCGPLS GRKTDMAINI
YTPGCYLLCH DDVIGSRRVS YILYLVDPDT PWKPEWGGAL RLFPVQEIKD KDGEVAKTPL
PDVSKVIPPA WNQLSFFAVQ PGESFHDVEE VYRAETKKQL EKEGGRIRMA ISGWFHIPQI
GEDGYIKGEE ERNAKNSGLM QLQGNPAQYD MPQPQVMKVD KSQASQGFDE ADLEFLLKYI
SPAYLVPDAL EEISETFNEM FEITLPDILG KKFAKRLRDY VEAEEKKPVP EDTPTIEKTS
PWRVAKPPHK ARYMYQQPSG PDQLRTSQEE SPITELLDIF LPSRQFRQWL QMATKTTVES
ADLLARRFRR GLDYTLATGH EGKARVEINL GFTPTNGWGE DEEEDPEEEA EEQNGKDVKG
KGKGKAKAVE KKKKEEEEVP EVGGQEIFMS GDDDADEDAA VYKTGGDDDD NILFFQAPTW
NKMTIVMRDS GALKFVKYIS KSAKGDRWDI SGAFEVEEDD DDDDDAAEDD DDEEEFQGFS
PKGTESESD
//
