ID B5LEC8_PHARH Unreviewed; 557 AA.
AC B5LEC8;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Astaxanthin synthase {ECO:0000313|EMBL:ACH73153.1};
GN Name=crtS {ECO:0000313|EMBL:ACH73153.1};
OS Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Cystofilobasidiales; Mrakiaceae; Phaffia.
OX NCBI_TaxID=264483 {ECO:0000313|EMBL:ACH73153.1};
RN [1] {ECO:0000313|EMBL:ACH73153.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Atx5 {ECO:0000313|EMBL:ACH73153.1};
RX PubMed=18769767;
RA Niklitschek M., Alcaino J., Barahona S., Sepulveda D., Lozano C.,
RA Carmona M., Marcoleta A., Martinez C., Lodato P., Baeza M., Cifuentes V.;
RT "Genomic organization of the structural genes controlling the astaxanthin
RT biosynthesis pathway of Xanthophyllomyces dendrorhous.";
RL Biol. Res. 41:93-108(2008).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; EU713462; ACH73153.1; -; Genomic_DNA.
DR AlphaFoldDB; B5LEC8; -.
DR SMR; B5LEC8; -.
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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11069; CYP_FUM15-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT BINDING 495
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:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 557 AA; 62689 MW; BC794CEC16F2A26A CRC64;
MFILVLLTGA LGLAAFSWAS IAFFSLYLAP RRSSLYNLQG PNHTNYFTGN FLDILSARTD
EEHAKYREKY GSTLRFAGIA GAPVLNSTDP KVFNHVMKEA YDYPKPGMAA RVLRIATGDG
VVTAEGEAHK RHRRIMIPSL SAQAVKSMVP IFLEKGMELV DKMMEDAAEK DMAVGESAGE
KKATRLETEG VDVKDWVGRA TLDVMALAGF DYKSDSLQNK TNELYVAFVG LTDGFAPTLD
SFKAIMWDFV PYFRTMKRRH EIPLTQGLAV SRRVGIELME QKKQAVLGSA SDQAVDKKDV
QGRDILSLLV RANIAANLPE SQKLSDEEVL AQISNLLFAG YETSSTVLTW MFHRLSEDKA
VQDKLREEIC QIDTDMPTLD ELNALPYLEA FVKESLRLDP PSPYANRECL KDEDFIPLAE
PVIGRDGSVI NEVRITKGTM VMLPLFNINR SKFIYGEDAE EFRPERWLED VTDSLNSIEA
PYGHQASFIS GPRACFGWRF AVAEMKAFLF VTLRRVQFEP IISHPEYEHI TLIISRPRIV
GREKEGYQMR LQVKPVE
//
