ID D2V9J7_NAEGR Unreviewed; 436 AA.
AC D2V9J7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC46600.1};
GN ORFNames=NAEGRDRAFT_65467 {ECO:0000313|EMBL:EFC46600.1};
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:EFC46600.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC46600.1,
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 NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG738858; EFC46600.1; -; Genomic_DNA.
DR RefSeq; XP_002679344.1; XM_002679298.1.
DR AlphaFoldDB; D2V9J7; -.
DR STRING; 5762.D2V9J7; -.
DR EnsemblProtists; EFC46600; EFC46600; NAEGRDRAFT_65467.
DR GeneID; 8859838; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_65467; -.
DR eggNOG; KOG1502; Eukaryota.
DR InParanoid; D2V9J7; -.
DR OrthoDB; 846192at2759; -.
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 CDD; cd08958; FR_SDR_e; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 46..314
FT /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF01073"
SQ SEQUENCE 436 AA; 49424 MW; 323071C7E9008A27 CRC64;
MGTNYPEDYS QQHHITTINQ QQELATNNME ETSLPLKENS KRKYCVIGGS GFLGSHLVMT
LLRRGHAVNL TVRNLGKVEN YEFIKKAACQ EGLDDNLQFF QADLAKDGSF YNAFLDCDGV
FATACPLDDA LTRNSSDPKS ELFDPIVNGV KNVVRECVKI RKEQNERNDS RRLKRLIFTS
SITAVSTDAL WDYKSKSWHY FDEAEWNDKA SLTQCTYAYC KTMSEREAFE LLKGEFSNTQ
LEIAAVLPST MFGPSIGIRK NIGMQPIISS IVDIPAHVRL FCPSVDVRDV ALAHCLVMEK
TSKPVNDQSN GFYIDHDYLA SNQERVIVHN NTICTRDICQ AISKYPQALQ ILEKKKLKLP
TQIPFLENTI GDKILLLGAY LTGPKPQYDL LRGMVGKELH FSNNYVKGKY GLEFTDLDQT
ILETVMHILE HDMHKL
//