ID A0A093DM89_9AVES Unreviewed; 298 AA.
AC A0A093DM89;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cytochrome P450 3A {ECO:0000256|RuleBase:RU368049};
DE EC=1.14.14.- {ECO:0000256|RuleBase:RU368049};
DE Flags: Fragment;
GN ORFNames=N339_06050 {ECO:0000313|EMBL:KFV02966.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV02966.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV02966.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV02966.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC In liver microsomes, this enzyme is involved in an NADPH-dependent
CC electron transport pathway. It oxidizes a variety of structurally
CC unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC {ECO:0000256|RuleBase:RU368049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000256|RuleBase:RU368049};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|RuleBase:RU368049};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU368049}. Microsome membrane
CC {ECO:0000256|RuleBase:RU368049}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU368049}.
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DR EMBL; KL226515; KFV02966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093DM89; -.
DR Proteomes; UP000053149; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24302:SF44; CYTOCHROME P450; 1.
DR PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01689; EP450IICYP3A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU368049};
KW Heme {ECO:0000256|RuleBase:RU368049}; Iron {ECO:0000256|RuleBase:RU368049};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU368049};
KW Microsome {ECO:0000256|ARBA:ARBA00022848, ECO:0000256|RuleBase:RU368049};
KW Monooxygenase {ECO:0000256|RuleBase:RU368049};
KW Oxidoreductase {ECO:0000256|RuleBase:RU368049};
KW Reference proteome {ECO:0000313|Proteomes:UP000053149};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV02966.1"
FT NON_TER 298
FT /evidence="ECO:0000313|EMBL:KFV02966.1"
SQ SEQUENCE 298 AA; 34152 MW; DC437DCF66351D99 CRC64;
KPDLMSKPML DSILCLRDDR WKYVRSLLTP AFSDTKLKEM IPLINQACDV LLCNLKVCAD
SGKAFDIQRC YNCFTLDVVG SVAFGTEVDS LKNPEDPFVK NCRTFFEMSL FKPLFILILS
FPFIMIPLLR ILPNKKQKEL NGFFIQTIKN AIVFRDQQDA SERRRDFLQW MLDSRSSADS
LADWCFDVIS PSATSRQNEE SLASRAPSEK VQKTLTDDEI AGQAFLFLIA GYETTTSTLS
FATYLLATNP ECQEKVLQEV DEFSAKHMVP DYQNVQELPY LDMVIAETLR MYPPAFRY
//
