ID Q6VT82_CARMA Unreviewed; 502 AA. AC Q6VT82; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-OCT-2024, entry version 78. DE SubName: Full=Cytochrome P450 CYP330A1 {ECO:0000313|EMBL:AAQ93009.1}; OS Carcinus maenas (Common shore crab) (Green crab). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; OC Eubrachyura; Portunoidea; Carcinidae; Carcinus. OX NCBI_TaxID=6759 {ECO:0000313|EMBL:AAQ93009.1}; RN [1] {ECO:0000313|EMBL:AAQ93009.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=14521903; DOI=10.1016/j.bbrc.2003.09.063; RA Rewitz K., Styrishave B., Andersen O.; RT "CYP330A1 and CYP4C39 enzymes in the shore crab Carcinus maenas: sequence RT and expression regulation by ecdysteroids and xenobiotics."; RL Biochem. Biophys. Res. Commun. 310:252-260(2003). CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971, CC ECO:0000256|PIRSR:PIRSR602401-1}; CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY328466; AAQ93009.1; -; mRNA. DR AlphaFoldDB; Q6VT82; -. DR GO; GO:0016020; C: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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR CDD; cd20651; CYP15A1-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR036396; Cyt_P450_sf. DR InterPro; IPR050182; Cytochrome_P450_fam2. DR PANTHER; PTHR24300:SF385; CYTOCHROME P450 306A1; 1. DR PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Heme {ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU000461}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR602401-1, KW ECO:0000256|RuleBase:RU000461}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..33 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 40..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 448 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:PIRSR602401-1" SQ SEQUENCE 502 AA; 57646 MW; D807AB18376B7AAE CRC64; MSSVFTWGTG LVGTWLPTFL LVLFITLLVL GMFGGRPKNF PPGLMILPVV GSFLSMPFGP SLEVLRGLRK KYGDMASFAI FGTRIVVVSS VNLMKEVFGL RASTDRPEVF FSTHRNRIMT DGRSTAIGVI GSSGQVWQEQ RRFMLHHLRD LGFGKSSYEP VMVEEIAELM DLLKKEEGRP LEVKLLFNRS VVNIIWAMVM GTRYHYGHDK LNKLMANFVH TAEFNALTPL YHIPHVFKIM HYLPRHSKGH RFMRRLINFI KEEIKEFMDN EELKNSDNFA AVYLREIEKK ENPNFNMDQL SALIFDLFVA GMETTSSALT TAVYLISKHP HVQRRLQEEL DEMVGKDRLP SFSDMDRLPY VQATIHEVQR VLNFVKFSLP HVANQDCKLG GYDIPKGTWL LANLDDALRS SEYWKNSLEF DPQNFLDENG KYKKNDAFMP FGVGKRVCAG ESLARLELFL FFTHLFQRFT FSLVEEHKPI AEDNPMFASP PEYTATIKCR SI //