C7111_SOLLC
ID C7111_SOLLC Reviewed; 501 AA.
AC Q1T7C2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Cytochrome P450 710A11 {ECO:0000303|PubMed:16531502};
DE EC=1.14.19.41 {ECO:0000269|PubMed:16531502};
DE AltName: Full=C-22 sterol desaturase {ECO:0000303|PubMed:16531502};
GN Name=CYP710A11 {ECO:0000303|PubMed:16531502};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|EMBL:BAE93156.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=16531502; DOI=10.1105/tpc.105.036012;
RA Morikawa T., Mizutani M., Aoki N., Watanabe B., Saga H., Saito S.,
RA Oikawa A., Suzuki H., Sakurai N., Shibata D., Wadano A., Sakata K.,
RA Ohta D.;
RT "Cytochrome P450 CYP710A encodes the sterol C-22 desaturase in Arabidopsis
RT and tomato.";
RL Plant Cell 18:1008-1022(2006).
CC -!- FUNCTION: Required to form the C-22 double bond in the sterol side
CC chain. Possesses in vitro C-22 desaturase activity toward beta-
CC sitosterol to produce stigmasterol. No activity with 24-epi-
CC campesterol. {ECO:0000269|PubMed:16531502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-
CC 5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+);
CC Xref=Rhea:RHEA:33467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18249, ChEBI:CHEBI:52972,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.19.41;
CC Evidence={ECO:0000269|PubMed:16531502};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for beta-sisterol {ECO:0000269|PubMed:16531502};
CC Note=kcat is 10 min(-1) for beta-sisterol.
CC {ECO:0000269|PubMed:16531502};
CC -!- PATHWAY: Steroid biosynthesis; sterol biosynthesis.
CC {ECO:0000269|PubMed:16531502}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- CAUTION: Was called CYP710A7 in EMBL:BAE93156. According to the
CC cytochrome P450 homepage, CYP710A7 is a rice cytochrome. {ECO:0000305}.
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DR EMBL; AB223043; BAE93156.1; -; mRNA.
DR AlphaFoldDB; Q1T7C2; -.
DR SMR; Q1T7C2; -.
DR STRING; 4081.Solyc02g070580.1.1; -.
DR PaxDb; Q1T7C2; -.
DR PRIDE; Q1T7C2; -.
DR eggNOG; KOG0157; Eukaryota.
DR BRENDA; 1.14.19.41; 3101.
DR UniPathway; UPA00766; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q1T7C2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Cytochrome P450 710A11"
FT /id="PRO_0000435506"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 445
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 501 AA; 57519 MW; 81A4E12C55A0DF9D CRC64;
MASIWGLLSP WIPYFISFIA FLLLLEQISY IKKKRFLPGP TLVFPFLGNV IPLVTNPTKF
WDLQSALAKS TSHGFSVNYI IGKFILYIHS TDLSHKVFAN VRPDAFHLIG HPFGKKLFGE
HNLIYMFGQE HKDLRRRIAP NFTPKALGTY TDIQQRIIIK HFKSWLDEAS KSPNTPIPLR
LLCRDMNLDT SQTVFVGPYL DGESRKRFNV DYNYFNVGLR KLPVDLPGFA FRNARLAVGR
LVDTLSVCVE QSLNKMKNEE EPTCLIDFWM QENLREINEA KINGLQKPFQ YSNKELGGYL
FDFLFAAQDA STSALLWAIV LLDSHPQVLE KVRSDVARFW SPESEEPLTA EMLTEMKYLE
AVAREIIRIR APATMVPHIA GEEFRLTEDY VIPKGTIVFP SVFDSSFQGF PEPEKFEPDR
FMEERQEERV YKKNFLALGA GPHACVGQKY AINHLMLIIA MFTALIDFKR HKTDGCDDIS
YIPTIAPKDD CKVFLAHRCT R
