AK2E4_BOMMO
ID AK2E4_BOMMO Reviewed; 308 AA.
AC H9JTG9;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Aldo-keto reductase AKR2E4;
DE EC=1.1.1.-;
DE AltName: Full=3-dehydroecdysone reductase;
DE AltName: Full=Aldo-keto reductase 2E;
GN Name=akr2e; Synonyms=AKR2E4;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN
RP COMPLEX WITH NADP, INDUCTION BY DIAZINON, FUNCTION, TISSUE SPECIFICITY,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Larva;
RX PubMed=24012638; DOI=10.1016/j.abb.2013.08.018;
RA Yamamoto K., Wilson D.K.;
RT "Identification, characterization, and crystal structure of an aldo-keto
RT reductase (AKR2E4) from the silkworm Bombyx mori.";
RL Arch. Biochem. Biophys. 538:156-163(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
CC -!- FUNCTION: NADP-dependent oxidoreductase with high 3-dehydroecdysone
CC reductase activity. May play a role in the regulation of molting. Has
CC lower activity with phenylglyoxal and isatin (in vitro). Has no
CC activity with NADH as cosubstrate. Has no activity with
CC nitrobenzaldehyde and 3-hydroxybenzaldehyde.
CC {ECO:0000269|PubMed:24012638}.
CC -!- ACTIVITY REGULATION: Subject to substrate inhibition by high levels of
CC 3-dehydroecdysone. {ECO:0000269|PubMed:24012638}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0044 mM for 3-dehydroecdysone {ECO:0000269|PubMed:24012638};
CC -!- TISSUE SPECIFICITY: Detected in hemolymph (at protein level). Detected
CC in larval ovary. {ECO:0000269|PubMed:24012638}.
CC -!- DEVELOPMENTAL STAGE: During larval development, expression in the
CC hemolymph increases at day 3 before the fourth ecdysis and then
CC decreases again. Levels increase again at day 8 and then decrease
CC again. Not detectable in pupae, or present at very low levels.
CC -!- INDUCTION: Up-regulated by the insecticide diazinon.
CC {ECO:0000269|PubMed:24012638}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB701383; BAL70378.1; -; mRNA.
DR RefSeq; NP_001296537.1; NM_001309608.1.
DR PDB; 3WCZ; X-ray; 1.30 A; A=1-308.
DR PDBsum; 3WCZ; -.
DR AlphaFoldDB; H9JTG9; -.
DR SMR; H9JTG9; -.
DR STRING; 7091.BGIBMGA012831-TA; -.
DR EnsemblMetazoa; BGIBMGA012831-RA; BGIBMGA012831-TA; BGIBMGA012831.
DR GeneID; 101743035; -.
DR KEGG; bmor:101743035; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; H9JTG9; -.
DR OMA; WHADSSY; -.
DR OrthoDB; 1016440at2759; -.
DR SABIO-RK; H9JTG9; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd19116; AKR_AKR2E1-5; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044488; AKR2E.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid metabolism; NADP; Oxidoreductase; Reference proteome;
KW Steroid metabolism.
FT CHAIN 1..308
FT /note="Aldo-keto reductase AKR2E4"
FT /id="PRO_0000425542"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 22..29
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24012638"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24012638"
FT BINDING 158..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24012638"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24012638"
FT BINDING 259..269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:24012638"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:3WCZ"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:3WCZ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:3WCZ"
SQ SEQUENCE 308 AA; 34353 MW; DF59F5F1C1C08336 CRC64;
MAVQAPCIQL NDGNTIPIVA LGTGRGTAKE SDSIDEVRQA VYWAIEAGYR HIDTAAVYQD
EEQVGQGIAE AIANGLVTRE ELFVTTKLWN DKHARDQVVP ALQESLKKLG LDYIDLYLIH
FPIATKPDDS PDNIDYLETW QGMQDARQLG LARSIGVSNF NATQITRLVS NSYIRPVINQ
IEVNPTNTQE PLVAHCQSLG IAVMAYSPFG FVVSRGQTGA PPPRSDDPTL TALANKYRKS
VGQILLRYLI DRGLIPIPKS TNKQRIAQNI DLFDFQLTFE EVAAINQFNK NHRVIDISDW
KDYPNYPN
