IVOC_EMENI
ID IVOC_EMENI Reviewed; 512 AA.
AC C8V7P3;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=N-acetyltryptophan 6-hydroxylase ivoC {ECO:0000303|PubMed:28108400};
DE EC=1.-.-.- {ECO:0000269|PubMed:28108400};
DE AltName: Full=Benzoate 4-monooxygenase {ECO:0000303|PubMed:18824241};
DE AltName: Full=Cytochrome P450 monooxygenase ivoC {ECO:0000303|PubMed:28108400};
DE AltName: Full=Ivory mutation-related protein C {ECO:0000305};
GN Name=ivoC {ECO:0000303|PubMed:18824241};
GN ORFNames=ANIA_10573 {ECO:0000312|EMBL:CBF77085.1};
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 FUNCTION.
RX DOI=10.1016/0031-9422(83)85048-1;
RA McCorkindale N.J., Hayes D., Johnston G.A., Clutterbuck A.J.;
RT "N-acetyl-6-hydroxytryptophan a natural substrate of a monophenol oxidase
RT from Aspergillus nidulans.";
RL Phytochemistry 22:1026-1028(1983).
RN [4]
RP FUNCTION.
RX PubMed=2126551; DOI=10.1099/00221287-136-9-1725;
RA Birse C.E., Clutterbuck A.J.;
RT "N-acetyl-6-hydroxytryptophan oxidase, a developmentally controlled phenol
RT oxidase from Aspergillus nidulans.";
RL J. Gen. Microbiol. 136:1725-1730(1990).
RN [5]
RP IDENTIFICATION.
RX PubMed=18824241; DOI=10.1016/j.fgb.2008.08.010;
RA Kelly D.E., Krasevec N., Mullins J., Nelson D.R.;
RT "The CYPome (Cytochrome P450 complement) of Aspergillus nidulans.";
RL Fungal Genet. Biol. 46:S53-S61(2009).
RN [6]
RP IDENTIFICATION OF THE IVO CLUSTER.
RX PubMed=23617571; DOI=10.1186/1471-2180-13-91;
RA Inglis D.O., Binkley J., Skrzypek M.S., Arnaud M.B., Cerqueira G.C.,
RA Shah P., Wymore F., Wortman J.R., Sherlock G.;
RT "Comprehensive annotation of secondary metabolite biosynthetic genes and
RT gene clusters of Aspergillus nidulans, A. fumigatus, A. niger and A.
RT oryzae.";
RL BMC Microbiol. 13:91-91(2013).
RN [7]
RP FUNCTION, AND PATHWAY.
RX PubMed=28108400; DOI=10.1016/j.fgb.2017.01.006;
RA Sung C.T., Chang S.L., Entwistle R., Ahn G., Lin T.S., Petrova V.,
RA Yeh H.H., Praseuth M.B., Chiang Y.M., Oakley B.R., Wang C.C.C.;
RT "Overexpression of a three-gene conidial pigment biosynthetic pathway in
RT Aspergillus nidulans reveals the first NRPS known to acetylate
RT tryptophan.";
RL Fungal Genet. Biol. 101:1-6(2017).
RN [8]
RP FUNCTION.
RX PubMed=31573806; DOI=10.1021/jacs.9b08898;
RA Hai Y., Jenner M., Tang Y.;
RT "Complete stereoinversion of L-tryptophan by a fungal single-module
RT nonribosomal peptide synthetase.";
RL J. Am. Chem. Soc. 141:16222-16226(2019).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the pathway that
CC mediates the biosynthesis of the gray-brown conidiophore pigment
CC (PubMed:23617571, PubMed:28108400). The first step of the pathway is
CC performed by the nonribosomal peptide synthetase ivoA that catalyzes
CC ATP-dependent unidirectional stereoinversion of L-tryptophan to D-
CC tryptophan with complete conversion (PubMed:31573806). While the
CC stereoinversion is catalyzed by the epimerization (E) domain of ivoA,
CC the terminal condensation (C) domain stereoselectively hydrolyzes D-
CC tryptophanyl-S-phosphopantetheine thioester and thus represents a non-
CC canonical C domain function (PubMed:31573806). D-tryptophan is
CC acetylated, probably by an endogenous acetyltransferase (Probable). N-
CC acetyltryptophan is further 6-hydroxylated into N-acetyl-6-
CC hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC
CC (PubMed:28108400). N-acetyl-6-hydroxytryptophan is substrate of the N-
CC acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown
CC conidiophore pigment (PubMed:2126551, PubMed:28108400, Ref.3).
CC {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:23617571,
CC ECO:0000269|PubMed:28108400, ECO:0000269|PubMed:31573806,
CC ECO:0000269|Ref.3, ECO:0000305|PubMed:31573806}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:28108400}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BN001303; CBF77085.1; -; Genomic_DNA.
DR AlphaFoldDB; C8V7P3; -.
DR SMR; C8V7P3; -.
DR STRING; 162425.CADANIAP00005790; -.
DR EnsemblFungi; CBF77085; CBF77085; ANIA_10573.
DR VEuPathDB; FungiDB:AN10573; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_14_4_1; -.
DR InParanoid; C8V7P3; -.
DR OMA; EPVIQAN; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000000560; Chromosome III.
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 PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="N-acetyltryptophan 6-hydroxylase ivoC"
FT /id="PRO_0000444122"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 453
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 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 512 AA; 58042 MW; F0E00EB92B11B4DE CRC64;
MLSLDLVFSF PAWALLLVLT LLYTLYLATT RLLLSPIRHI PGPTLAALSF WPEFYYDVVQ
RGQYFRQIDK MHQTYGPLVR INPFEIHIQD PSFYPVLYTG PTRRRHKWLW AARMFGNNTS
AFATVRHEHH RLRRSALNPL FSKSAIQRLT PHLQHTLARL CSRLDGFAFT RQDVDLGIGL
TAFAADVITE YCFGQSLELI GKDNFGKEWI DMVSAPSELG HLVKQCPWIL VVCKWAPKAL
VRALLPGVAL LFQIQERMSA QIQPLVDRAA AVDKPADPLT VFDFLLSSTL PQHEKTVDRL
KGEGQTLIGA GTLTTGNALK TIIFHVLNDP DIFRKLRAEV DGALENMDIL SMSDTAYLER
LPYLSACIKE GLRISYGVTH RLQLIAEEPL IYSGVTIPAG TPVGMTSIFM HDNPVVFPQP
REFRPERWFE ADFETVQAMN RHFVPFSKGS RMCLGMNLAY AEIYLVLAVL FRRYEISLSG
VTREDIEMAH DFFDPAPKEG ARGLIVQLQK RG
