DHRS4_CAEEL
ID DHRS4_CAEEL Reviewed; 260 AA.
AC G5EGA6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Dehydrogenase/reductase SDR family member 4 {ECO:0000250|UniProtKB:Q9BTZ2};
DE EC=1.1.1.184 {ECO:0000305|PubMed:21300042};
GN Name=dhrs-4 {ECO:0000312|WormBase:F54F3.4};
GN ORFNames=F54F3.4 {ECO:0000312|WormBase:F54F3.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|WormBase:F54F3.4};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21300042; DOI=10.1016/j.cbi.2011.01.034;
RA Kisiela M., El-Hawari Y., Martin H.J., Maser E.;
RT "Bioinformatic and biochemical characterization of DCXR and DHRS2/4 from
RT Caenorhabditis elegans.";
RL Chem. Biol. Interact. 191:75-82(2011).
CC -!- FUNCTION: Catalyzes the reduction of isatin, 4-oxonon-2-enal, 9,10-
CC phenanthrenequinone, menadione, 2,3-hexaenadione, 3,4-hexanedione and
CC 2,3-heptanedione. {ECO:0000269|PubMed:21300042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.184; Evidence={ECO:0000305|PubMed:21300042};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for isatin (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:21300042};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255}.
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DR EMBL; Z79696; CAB01974.1; -; Genomic_DNA.
DR EMBL; Z81592; CAB01974.1; JOINED; Genomic_DNA.
DR PIR; T22676; T22676.
DR RefSeq; NP_506230.1; NM_073829.5.
DR PDB; 5OJG; X-ray; 1.90 A; A/B=1-260.
DR PDB; 5OJI; X-ray; 1.60 A; A/B=1-260.
DR PDBsum; 5OJG; -.
DR PDBsum; 5OJI; -.
DR AlphaFoldDB; G5EGA6; -.
DR SMR; G5EGA6; -.
DR BioGRID; 44791; 5.
DR STRING; 6239.F54F3.4; -.
DR EPD; G5EGA6; -.
DR PaxDb; G5EGA6; -.
DR PeptideAtlas; G5EGA6; -.
DR PRIDE; G5EGA6; -.
DR EnsemblMetazoa; F54F3.4.1; F54F3.4.1; WBGene00010063.
DR GeneID; 179772; -.
DR KEGG; cel:CELE_F54F3.4; -.
DR CTD; 179772; -.
DR WormBase; F54F3.4; CE19894; WBGene00010063; dhrs-4.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; G5EGA6; -.
DR OMA; VGTLGKQ; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; G5EGA6; -.
DR Reactome; R-CEL-5365859; RA biosynthesis pathway.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR SABIO-RK; G5EGA6; -.
DR PRO; PR:G5EGA6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010063; Expressed in larva and 4 other tissues.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..260
FT /note="Dehydrogenase/reductase SDR family member 4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431306"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT BINDING 14..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:5OJI"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:5OJI"
FT TURN 212..218
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:5OJI"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5OJI"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:5OJI"
SQ SEQUENCE 260 AA; 27590 MW; E43FD36F5EDBA7F4 CRC64;
MPSNCRRFEG KVAIVTAATK GIGLAIAERL LDEGASVVIG SRNQKNVDEA IEYLKNKGLT
KVAGIAGHIA STDDQKKLVD FTLQKFGKIN ILVNNHGINP AFGHILEVSD QVWDKLFEVN
VKAGFQMTKL VHPHIAKEGG GAIIFNASYS AYKSPPGIAA YGVTKTTLVG LTRALAMGLA
KDNIRVNGIA PGVIKTKMSQ VLWDGGEDAE KELTDIQEIA LGRLGVPDDC AGTVAYLASD
DSSYITGEMI IIAGGVQARL
