NVD_BOMMO
ID NVD_BOMMO Reviewed; 453 AA.
AC Q1JUZ2; H9IWP6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cholesterol 7-desaturase nvd;
DE EC=1.14.19.21 {ECO:0000269|PubMed:21632547};
DE AltName: Full=Neverland {ECO:0000303|PubMed:21632547};
DE Short=Nvd_Bm {ECO:0000303|PubMed:21632547};
DE AltName: Full=Rieske-domain protein Neverland {ECO:0000312|EMBL:BAE94192.1};
GN Name=nvd-Bm {ECO:0000312|EMBL:BAE94192.1};
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].
RC STRAIN=Kinshu X Showa {ECO:0000312|EMBL:BAE94192.1};
RX PubMed=16763204; DOI=10.1242/dev.02428;
RA Yoshiyama T., Namiki T., Mita K., Kataoka H., Niwa R.;
RT "Neverland is an evolutionally conserved Rieske-domain protein that is
RT essential for ecdysone synthesis and insect growth.";
RL Development 133:2565-2574(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000312|Proteomes:UP000005204};
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21632547; DOI=10.1074/jbc.m111.244384;
RA Yoshiyama-Yanagawa T., Enya S., Shimada-Niwa Y., Yaguchi S., Haramoto Y.,
RA Matsuya T., Shiomi K., Sasakura Y., Takahashi S., Asashima M., Kataoka H.,
RA Niwa R.;
RT "The conserved Rieske oxygenase DAF-36/Neverland is a novel cholesterol-
RT metabolizing enzyme.";
RL J. Biol. Chem. 286:25756-25762(2011).
CC -!- FUNCTION: Catalyzes the production of 7-dehydrocholesterol (7-DHC or
CC cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating)
CC at the C7-C8 single bond of cholesterol. Essential regulator of steroid
CC biosynthesis as this reaction is the first step in the synthesis of the
CC steroid hormone Delta(7)-dafachronic acid.
CC {ECO:0000269|PubMed:21632547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADPH + O2 = 7-dehydrocholesterol + 2 H2O
CC + NADP(+); Xref=Rhea:RHEA:45024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.19.21; Evidence={ECO:0000269|PubMed:21632547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45025;
CC Evidence={ECO:0000305|PubMed:21632547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O
CC + NAD(+); Xref=Rhea:RHEA:51644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17759,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.19.21;
CC Evidence={ECO:0000269|PubMed:21632547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51645;
CC Evidence={ECO:0000305|PubMed:21632547};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- PATHWAY: Steroid hormone biosynthesis; dafachronic acid biosynthesis.
CC {ECO:0000305|PubMed:21632547}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cholesterol 7-desaturase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BABH01021056; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB232986; BAE94192.1; -; mRNA.
DR EMBL; BABH01021056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001037626.1; NM_001044161.1.
DR AlphaFoldDB; Q1JUZ2; -.
DR SMR; Q1JUZ2; -.
DR STRING; 7091.BGIBMGA001678-TA; -.
DR SwissLipids; SLP:000001121; -.
DR GeneID; 733067; -.
DR KEGG; bmor:733067; -.
DR CTD; 5740633; -.
DR eggNOG; ENOG502QS20; Eukaryota.
DR HOGENOM; CLU_037178_0_0_1; -.
DR OrthoDB; 1199207at2759; -.
DR BioCyc; MetaCyc:MON-18095; -.
DR BRENDA; 1.14.19.21; 890.
DR BRENDA; 1.3.1.21; 890.
DR UniPathway; UPA01020; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR045605; KshA-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF19298; KshA_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cholesterol metabolism; Iron; Iron-sulfur; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..453
FT /note="Cholesterol 7-desaturase nvd"
FT /id="PRO_0000452606"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..229
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 167
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 169
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 187
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 190
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 140
FT /note="V -> A (in Ref. 1; BAE94192)"
FT CONFLICT 227
FT /note="I -> V (in Ref. 1; BAE94192)"
FT CONFLICT 250
FT /note="D -> E (in Ref. 1; BAE94192)"
FT CONFLICT 362
FT /note="A -> V (in Ref. 1; BAE94192)"
FT CONFLICT 442
FT /note="S -> G (in Ref. 1; BAE94192)"
SQ SEQUENCE 453 AA; 50950 MW; ADA5D4AADB19A3AF CRC64;
MADRQHFPSA ITEAVSSNTA CPDTGPKAET TNIFLLLQRN ITIESSKHVF SSIVEYILIL
TLMFAFSAIL YVIYKSYISP VFYKKELTEV GFDHIPQGPD KGRRISRAQA SRRMGSKLPP
PYPNGWFAVA ETRELKVGSV LSIDALGQNL CVYRGEDGLA RCVDAYCPHL GANLAVGGTV
RGSCIECPFH KWRFNAAGTC VSLPGSDIAP KGVSIRTWCV VETDGAIWIW HDAEGREPLW
EITDPPELKD FGYRGRNEFE VSAHIQEIPE NGADVPHLNA VHSSSLLSDL GERYPVLHEI
IGRHVWNADW TKSDDHTSLM HITQEYKVLK YDLARIDVKV TQIGPGHVRL FLKTSVGPFY
IAQSVTPLGP LLQKVIHRVY SPAYNAPVGA FLVRCEAYMF ERDVTIWNSK RFVSAPAYVK
TDKTIRTFRN WFGQFYSEHS LSFRDALQNP LDW
