ID   C71A1_ZINZE             Reviewed;         513 AA.
AC   E3W9C4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Alpha-humulene 10-hydroxylase {ECO:0000303|PubMed:20730551};
DE            EC=1.14.14.113 {ECO:0000269|PubMed:20730551};
GN   Name=CYP71BA1 {ECO:0000303|PubMed:20730551};
OS   Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=311405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20730551; DOI=10.1007/s00018-010-0506-4;
RA   Yu F., Okamoto S., Harada H., Yamasaki K., Misawa N., Utsumi R.;
RT   "Zingiber zerumbet CYP71BA1 catalyzes the conversion of alpha-humulene to
RT   8-hydroxy-alpha-humulene in zerumbone biosynthesis.";
RL   Cell. Mol. Life Sci. 68:1033-1040(2011).
CC   -!- FUNCTION: Catalyzes the conversion of alpha-humulene to 10-hydroxy-
CC       alpha-humulene in the second step of zerumbone biosynthesis, a
CC       predominating potential multi-anticancer agent.
CC       {ECO:0000269|PubMed:20730551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-humulene + O2 + reduced [NADPH--hemoprotein reductase] =
CC         10-hydroxy-alpha-humulene + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:32491, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:5768, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:63893; EC=1.14.14.113;
CC         Evidence={ECO:0000269|PubMed:20730551};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest level in rhizomes and much
CC       less in leaves. Not expressed in stems. {ECO:0000269|PubMed:20730551}.
CC   -!- MISCELLANEOUS: The recommended numbering of humulene gives 10-hydroxy-
CC       alpha-humulene as the product rather than 8-hydroxy-alpha-humulene as
CC       used by the literature.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB331234; BAJ39893.1; -; mRNA.
DR   AlphaFoldDB; E3W9C4; -.
DR   SMR; E3W9C4; -.
DR   KEGG; ag:BAJ39893; -.
DR   BRENDA; 1.14.14.113; 12510.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102068; F:alpha-humulene 10-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Alpha-humulene 10-hydroxylase"
FT                   /id="PRO_0000418750"
FT   TRANSMEM        4..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   BINDING         452
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"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   513 AA;  57798 MW;  D7DE5F757C46C25C CRC64;
     MEAISLFSPF FFITLFLGFF ITLLIKRSSR SSVHKQQVLL ASLPPSPPRL PLIGNIHQLV
     GGNPHRILLQ LARTHGPLIC LRLGQVDQVV ASSVEAVEEI IKRHDLKFAD RPRDLTFSRI
     FFYDGNAVVM TPYGGEWKQM RKIYAMELLN SRRVKSFAAI REDVARKLTG EIAHKAFAQT
     PVINLSEMVM SMINAIVIRV AFGDKCKQQA YFLHLVKEAM SYVSSFSVAD MYPSLKFLDT
     LTGLKSKLEG VHGKLDKVFD EIIAQRQAAL AAEQAEEDLI IDVLLKLKDE GNQEFPITYT
     SVKAIVMEIF LAGTETSSSV IDWVMSELIK NPKAMEKVQK EMREAMQGKT KLEESDIPKF
     SYLNLVIKET LRLHPPGPLL FPRECRETCE VMGYRVPAGA RLLINAFALS RDEKYWGSDA
     ESFKPERFEG ISVDFKGSNF EFMPFGAGRR ICPGMTFGIS SVEVALAHLL FHFDWQLPQG
     MKIEDLDMME VSGMSATRRS PLLVLAKLII PLP