ID U4U2X8_DENPD Unreviewed; 756 AA.
AC U4U2X8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN ORFNames=D910_02374 {ECO:0000313|EMBL:ERL84951.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL84951.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL84951.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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=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 -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC {ECO:0000256|RuleBase:RU280818}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541}.
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DR EMBL; KB631644; ERL84951.1; -; Genomic_DNA.
DR AlphaFoldDB; U4U2X8; -.
DR STRING; 77166.U4U2X8; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10856; CORONIN; 1.
DR PANTHER; PTHR10856:SF0; CORONIN-LIKE PROTEIN; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR Pfam; PF00400; WD40; 3.
DR Pfam; PF16300; WD40_4; 1.
DR SMART; SM01166; DUF1899; 1.
DR SMART; SM01167; DUF1900; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280818};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 9..73
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 82..116
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 132..174
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 756 AA; 84764 MW; 8E52C7AADA19BF9F CRC64;
MTNNQIWFKG VRSSKFRHVY GEPAKRDKCY ENIQITKNAH DSQFCAVNPK FLAVVTEVAG
GGAYIVVPIN CTGRLDFNAS RVTGHSGPIL DIKWNPFNDN VIASCSDDCT IKLWHIPDDG
LAMHLNDWLV ELQGHKRRVA YIEWHPVAEN ILFSAGFDHL IILWDIERGE AINVIDCHPD
AIHSMSLNRD GSLLATTCKD KRLRVIEPRS GIVKSEGICH EGSKASKVVY LGSTGRLLTT
GFSRHSDRRY AVWDENNLSS PLFGDTIDSS SGIVFPFYDP DTNIVFLAGK GDGNIRFYEI
CDESPYIHYL SQVISGNPQR GLGFMPKRGL NTLQCEIYRF YKLHATKGLC EPISMVVPRK
SDQFHEDLYP DTAAAKPSLS AQEWIKGANA PPVLMSMRTG QSLALDIQAI KQRKFVTKTK
EAPVIDNNKR KFQFLSTETV PDYRPKDVQD EKSKKTTTNQ TTKFQQLQQR WSSTIEEPGK
DIPLFKEINS IGDNILTEHD LRLAYQIQSD EVKKLKKQLS NSEHRQNMQK STVKCRIGPS
ILNADLSQLH AESRRLLDNG ADYLHLDVMD GHFVPNLTFG HPLVKCLRKN IPNAFFETHM
MVQDPQKWIE PMADAGVSQY TFHIEPVIKE VLPICRKVRE AGMKVGLALK PGTGIEAVRQ
YIDHADMILI MTVEPGFGGQ TFMADMMPKV QWLRHNYPLL DIEVDGGVGL NTITACAEAG
ANMIVGGTAI IGACDQRSVI ASLRETVESS IHKCNV
//
