ALNH_EMENI
ID ALNH_EMENI Reviewed; 546 AA.
AC C8VJR0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Cytochrome P450 monooxygenase alnH {ECO:0000303|PubMed:30339758};
DE EC=1.-.-.- {ECO:0000305|PubMed:30339758};
DE AltName: Full=Asperlin biosynthesis cluster protein HA {ECO:0000303|PubMed:30339758};
GN Name=alnH {ECO:0000303|PubMed:30339758}; ORFNames=ANIA_11192;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30339758; DOI=10.1021/acschembio.8b00679;
RA Grau M.F., Entwistle R., Chiang Y.M., Ahuja M., Oakley C.E., Akashi T.,
RA Wang C.C.C., Todd R.B., Oakley B.R.;
RT "Hybrid transcription factor engineering activates the silent secondary
RT metabolite gene cluster for (+)-asperlin in Aspergillus nidulans.";
RL ACS Chem. Biol. 13:3193-3205(2018).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of asperlin, a polyketide showing anti-
CC inflammatory, antitumor and antibiotic activities (PubMed:30339758).
CC The first step of the asperlin biosynthesis is the production of the
CC intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide
CC synthase alnA with cleavage of the PKS product by the esterase alnB
CC (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to
CC asperlin via several steps involving the remaining enzymes from the
CC cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is controlled by the asperlin biosynthesis
CC cluster-specific transcription factor alnR.
CC {ECO:0000269|PubMed:30339758}.
CC -!- DISRUPTION PHENOTYPE: Fully eliminates the production of asperlin.
CC {ECO:0000269|PubMed:30339758}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BN001306; CBF82292.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VJR0; -.
DR SMR; C8VJR0; -.
DR STRING; 227321.C8VJR0; -.
DR EnsemblFungi; CBF82292; CBF82292; ANIA_11192.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_2_3_1; -.
DR InParanoid; C8VJR0; -.
DR OMA; CAMIGFA; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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 SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..546
FT /note="Cytochrome P450 monooxygenase alnH"
FT /id="PRO_0000445943"
FT TRANSMEM 11..31
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"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 546 AA; 62135 MW; 1D0EB9978A0BD6BE CRC64;
MTMAALDVFN VPYSVPLLGS TVVILIGFIA IKALRVGSRP KGLPPGPPTE FIWGNTKQID
LFYPQYQYRK WAQQYGPVYT VMLGDTAHVV VSGLRDVRDI FIKQGASSQN RPPSRFQLLM
RDGFFPGLNN GEKWRQSRRM WQAVLNNSAA KQYLPYQELE TRQLLFDLLR APTEWRDHIE
RYSNSVAMTM VNGRRIIDAA DPRVKETIQD LYDLAETGVR GAFLDSWPFL WKLPEWMFPV
CRQARKIAAK HREYIWRNYS DVAKRTSQGE VLPSVNHAIQ EKLKQGWPGV SEIEGAEIGH
HLLTGTTDTT ASTLINWVAA MCLHPEAQKK AQEEIDRVVG PNRLPTDADA ANLPYVQQVI
QEAQRWITAV PLSLPRAANA PVHWGKYTIP EETGLIMNSH ALHNDPDIFP EPDKFKPERW
EGKPNASSNG DAQLLFTFGA GRRVCPGQHL AERSLFLVIS HWLWGFDTLQ ATDDDKNKIP
IDKDDLRPGF IVCLNPFPAK ITPRTAQHRE LIERIWKEEL EVSLDESQQW KATPEGIARL
LERVGK
