MSMOB_DICDI
ID MSMOB_DICDI Reviewed; 270 AA.
AC Q55D54;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Putative methylsterol monooxygenase DDB_G0269788;
DE EC=1.14.18.9;
DE AltName: Full=C-4 methylsterol oxidase;
GN ORFNames=DDB_G0269788;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-
CC [cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-
CC cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O;
CC Xref=Rhea:RHEA:55220, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16455, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:58387; EC=1.14.18.9;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 3/6.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72244.1; -; Genomic_DNA.
DR RefSeq; XP_646277.1; XM_641185.1.
DR AlphaFoldDB; Q55D54; -.
DR SMR; Q55D54; -.
DR STRING; 44689.DDB0304895; -.
DR PaxDb; Q55D54; -.
DR EnsemblProtists; EAL72244; EAL72244; DDB_G0269788.
DR GeneID; 8617233; -.
DR KEGG; ddi:DDB_G0269788; -.
DR dictyBase; DDB_G0269788; -.
DR eggNOG; KOG0873; Eukaryota.
DR HOGENOM; CLU_047036_5_3_1; -.
DR InParanoid; Q55D54; -.
DR OMA; IVHEFIY; -.
DR PhylomeDB; Q55D54; -.
DR Reactome; R-DDI-192105; Synthesis of bile acids and bile salts.
DR UniPathway; UPA00770; UER00756.
DR PRO; PR:Q55D54; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; NAD; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..270
FT /note="Putative methylsterol monooxygenase DDB_G0269788"
FT /id="PRO_0000380109"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 118..249
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 132..136
FT /note="Histidine box-1"
FT /evidence="ECO:0000250"
FT MOTIF 145..149
FT /note="Histidine box-2"
FT /evidence="ECO:0000250"
FT MOTIF 224..230
FT /note="Histidine box-3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 31952 MW; F8805C799069A72C CRC64;
MESLSLKFIE PYWFKFVDYY GEDFLITYGT FIAHEVFYFG SFIPFFLCDF MPFLQKYKIQ
PTKKNEWKTQ FNCIFKVLMT HIFVQLPMMY IFDPAIKAIG LSARAPLPSI PYLIFTIACC
FLIEDFYFYW VHRALHHGFW YKHIHKVHHD HAAPFGMTAE YAHPLETVIL GVGTVIGPFL
FSRDLFTLWV WLGTRLFQTV ECHSGYDFPW NPTKLIPFWG GSHFHDFHHE TFVGNYSSTF
TYLDKIFGTS DKYYSRKQIR DSKLAAGKSE
