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Database: UniProt
Entry: D2V043_NAEGR
LinkDB: D2V043_NAEGR
Original site: D2V043_NAEGR 
ID   D2V043_NAEGR            Unreviewed;       315 AA.
AC   D2V043;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC49465.1};
GN   ORFNames=NAEGRDRAFT_45618 {ECO:0000313|EMBL:EFC49465.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC49465.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC49465.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family.
CC       {ECO:0000256|RuleBase:RU004475}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00023445}.
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DR   EMBL; GG738847; EFC49465.1; -; Genomic_DNA.
DR   RefSeq; XP_002682209.1; XM_002682163.1.
DR   AlphaFoldDB; D2V043; -.
DR   STRING; 5762.D2V043; -.
DR   EnsemblProtists; EFC49465; EFC49465; NAEGRDRAFT_45618.
DR   GeneID; 8856462; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_45618; -.
DR   eggNOG; KOG1502; Eukaryota.
DR   InParanoid; D2V043; -.
DR   OMA; VADENSW; -.
DR   OrthoDB; 1694166at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366:SF564; 3BETA_HSD DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          4..245
FT                   /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01073"
SQ   SEQUENCE   315 AA;  35397 MW;  A3D68D3215F38C3B CRC64;
     MFVAVTGASG YIAGHIVKQL LENGHRVRGV VRDLSNKSKY DYLEKFANLE NQLEFVQVND
     QNYENAFVGV DAVIHTATPY IYTAKDPQKE IVEPAVNLTR GVIEAALKNQ VKRVVITSSG
     GAIFSFPVPQ GKIFTSNDWN LQSNLTNNPY FYSKRLAEEE AWRLYKENSD KIEIVVVNPV
     YVLGPTLNPF INTSVENLKK YLLGEHETVQ VGGIAIVDVR NVATAHVLAV EKKEAAGKRL
     ICSGQVCNWS DIPKTLKQQF PQYAVSKYTE FPEATTYGMD TQPLKDLGLV EYYSFEQTIR
     DTVESLLEHN LIEKL
//
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