IVOB_EMENI
ID IVOB_EMENI Reviewed; 366 AA.
AC Q5BGU9; C8VUM5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=N-acetyl-6-hydroxytryptophan oxidase ivoB {ECO:0000303|PubMed:28108400};
DE Short=AHTase ivoB {ECO:0000303|PubMed:28108400};
DE EC=1.14.-.- {ECO:0000269|PubMed:28108400};
DE AltName: Full=Ivory mutation-related protein B {ECO:0000303|Ref.4};
DE AltName: Full=Monophenol oxidase {ECO:0000303|PubMed:2126551};
DE Flags: Precursor;
GN Name=ivoB {ECO:0000303|PubMed:28108400}; ORFNames=ANIA_00231;
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 PROTEIN SEQUENCE OF 19-53, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [5]
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 [6]
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 [7]
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.4).
CC {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:23617571,
CC ECO:0000269|PubMed:28108400, ECO:0000269|PubMed:31573806,
CC ECO:0000269|Ref.4, ECO:0000305|PubMed:31573806}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- ACTIVITY REGULATION: Activity is inhibited by 2,3-dihydroxynaphthalene,
CC phenylhydrazine, diethyl dithiocarbamate and 8-hydroxyquinolene
CC (PubMed:2126551). {ECO:0000269|PubMed:2126551}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:2126551};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:2126551,
CC ECO:0000269|PubMed:28108400, ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of the gray-brown
CC conidiophore pigment and leads to 'ivory' (colorless) conidiophores and
CC accumulation of N-acetyl-6-hydroxytryptophan (AHT) (PubMed:2126551).
CC {ECO:0000269|PubMed:2126551}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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; BN001308; CBF89919.1; -; Genomic_DNA.
DR RefSeq; XP_657835.1; XM_652743.1.
DR AlphaFoldDB; Q5BGU9; -.
DR SMR; Q5BGU9; -.
DR STRING; 162425.CADANIAP00002495; -.
DR EnsemblFungi; CBF89919; CBF89919; ANIA_00231.
DR EnsemblFungi; EAA66104; EAA66104; AN0231.2.
DR GeneID; 2876009; -.
DR KEGG; ani:AN0231.2; -.
DR eggNOG; ENOG502RM4B; Eukaryota.
DR HOGENOM; CLU_035914_0_0_1; -.
DR InParanoid; Q5BGU9; -.
DR OMA; YIDAVWC; -.
DR OrthoDB; 518234at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Glycoprotein; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2126551"
FT CHAIN 19..366
FT /note="N-acetyl-6-hydroxytryptophan oxidase ivoB"
FT /evidence="ECO:0000255"
FT /id="PRO_5010255833"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 291
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 366 AA; 40299 MW; 93349C583E480373 CRC64;
MHLLSSLAAL AAAITVAFAD VQQCNAENAS VRKEWGSLTP DEQLGYIDAV WCLRSLPSRL
PNEQYPGVQD RVDDFVATHI NLTMVIHRNA PFLPWHRQYI HLWETALREE CGYNGTVPYW
NWTKNPDLYT NPVFDTTQSP ETSLSLSGDG AYVAPSPTDP DPDPGLDFAP GRGGGCVLDG
PFKDWPVRMG PFSAAQAYPY APVPENAFAH NPRCLQRNLD VARIQYYNNP SVLESLLAAP
SIAVFQDILD RTIPGTWQQA IGAHGGGHIS VGPTLADVFA SPQDPVFMLH HGFIDLLWDA
WQRSGSDTGE GTDRMRALNG TTMYTNPPGA EEATLDTVME FGVLGSPKKI GEVMDIRGGE
YCYRYE
