ARP1_ASPFU
ID ARP1_ASPFU Reviewed; 168 AA.
AC O14434; Q4WZB0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Scytalone dehydratase arp1 {ECO:0000305|PubMed:19703288};
DE EC=4.2.1.94 {ECO:0000305|PubMed:19703288};
DE AltName: Full=Conidial pigment biosynthesis oxidase arp1 {ECO:0000305};
GN Name=arp1 {ECO:0000303|PubMed:9383199}; ORFNames=AFUA_2G17580;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=B-5233;
RX PubMed=9383199; DOI=10.1046/j.1365-2958.1997.5681921.x;
RA Tsai H.-F., Washburn R.G., Chang Y.C., Kwon-Chung K.J.;
RT "Aspergillus fumigatus arp1 modulates conidial pigmentation and complement
RT deposition.";
RL Mol. Microbiol. 26:175-183(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP FUNCTION.
RX PubMed=10515939; DOI=10.1128/jb.181.20.6469-6477.1999;
RA Tsai H.F., Wheeler M.H., Chang Y.C., Kwon-Chung K.J.;
RT "A developmentally regulated gene cluster involved in conidial pigment
RT biosynthesis in Aspergillus fumigatus.";
RL J. Bacteriol. 181:6469-6477(1999).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=19703288; DOI=10.1186/1471-2180-9-177;
RA Pihet M., Vandeputte P., Tronchin G., Renier G., Saulnier P.,
RA Georgeault S., Mallet R., Chabasse D., Symoens F., Bouchara J.P.;
RT "Melanin is an essential component for the integrity of the cell wall of
RT Aspergillus fumigatus conidia.";
RL BMC Microbiol. 9:177-177(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19156203; DOI=10.1371/journal.pone.0004224;
RA Jackson J.C., Higgins L.A., Lin X.;
RT "Conidiation color mutants of Aspergillus fumigatus are highly pathogenic
RT to the heterologous insect host Galleria mellonella.";
RL PLoS ONE 4:E4224-E4224(2009).
RN [6]
RP FUNCTION.
RX PubMed=20145078; DOI=10.1128/aac.01504-09;
RA Ben-Ami R., Lewis R.E., Leventakos K., Latge J.P., Kontoyiannis D.P.;
RT "Cutaneous model of invasive aspergillosis.";
RL Antimicrob. Agents Chemother. 54:1848-1854(2010).
RN [7]
RP FUNCTION.
RX PubMed=21747802; DOI=10.3389/fmicb.2011.00096;
RA Thywissen A., Heinekamp T., Dahse H.M., Schmaler-Ripcke J., Nietzsche S.,
RA Zipfel P.F., Brakhage A.A.;
RT "Conidial dihydroxynaphthalene melanin of the human pathogenic fungus
RT Aspergillus fumigatus interferes with the host endocytosis pathway.";
RL Front. Microbiol. 2:96-96(2011).
RN [8]
RP FUNCTION.
RX PubMed=21573171; DOI=10.1371/journal.pone.0019591;
RA Mech F., Thywissen A., Guthke R., Brakhage A.A., Figge M.T.;
RT "Automated image analysis of the host-pathogen interaction between
RT phagocytes and Aspergillus fumigatus.";
RL PLoS ONE 6:E19591-E19591(2011).
RN [9]
RP FUNCTION.
RX PubMed=24818666; DOI=10.1128/iai.01726-14;
RA Bayry J., Beaussart A., Dufrene Y.F., Sharma M., Bansal K., Kniemeyer O.,
RA Aimanianda V., Brakhage A.A., Kaveri S.V., Kwon-Chung K.J., Latge J.P.,
RA Beauvais A.;
RT "Surface structure characterization of Aspergillus fumigatus conidia
RT mutated in the melanin synthesis pathway and their human cellular immune
RT response.";
RL Infect. Immun. 82:3141-3153(2014).
RN [10]
RP FUNCTION.
RX PubMed=25684622; DOI=10.1111/1462-2920.12808;
RA Hillmann F., Novohradska S., Mattern D.J., Forberger T., Heinekamp T.,
RA Westermann M., Winckler T., Brakhage A.A.;
RT "Virulence determinants of the human pathogenic fungus Aspergillus
RT fumigatus protect against soil amoeba predation.";
RL Environ. Microbiol. 17:2858-2869(2015).
RN [11]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26972005; DOI=10.1016/j.celrep.2016.02.059;
RA Upadhyay S., Xu X., Lowry D., Jackson J.C., Roberson R.W., Lin X.;
RT "Subcellular compartmentalization and trafficking of the biosynthetic
RT machinery for fungal melanin.";
RL Cell Rep. 14:2511-2518(2016).
CC -!- FUNCTION: Scytalone dehydratase; part of the gene cluster that mediates
CC the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green
CC pigment and a structural component of the conidial wall
CC (PubMed:10515939, PubMed:19156203). The first step of the pathway is
CC the production of the heptaketide naphtopyrone YWA1 by the polyketide
CC synthase alb1 though condensation of acetyl-CoA with malonyl-CoA
CC (PubMed:10515939). The naphtopyrone YWA1 is then converted to the
CC pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the
CC heptaketide hydrolyase ayg1 though chain-length shortening
CC (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene
CC reductase arp2 to yield scytalone (PubMed:10515939). The scytalone
CC dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939).
CC 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to
CC yield vermelone (PubMed:10515939). Vermelone is further converted by
CC the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the
CC laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-
CC melanin biosynthesis appears to be initiated in endosomes where early
CC enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading
CC to melanin deposition on the cell surface where late enzymes (abr1 and
CC abr2) localize (PubMed:26972005). DHN-melanin is an important
CC structural component of the outer cell wall and is required for the
CC presence of conidial surface hydrophobins (PubMed:19703288). DHN-
CC melanin also plays a crucial role in fungal virulence, including a
CC protective role against the host's immune defenses (PubMed:19156203,
CC PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666).
CC DHN-melanin protects also conidia against amoeba predation
CC (PubMed:25684622). {ECO:0000269|PubMed:10515939,
CC ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:19703288,
CC ECO:0000269|PubMed:20145078, ECO:0000269|PubMed:21573171,
CC ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666,
CC ECO:0000269|PubMed:25684622, ECO:0000269|PubMed:26972005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=scytalone = 1,3,8-trihydroxynaphthalene + H2O;
CC Xref=Rhea:RHEA:24396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16945,
CC ChEBI:CHEBI:18393; EC=4.2.1.94;
CC Evidence={ECO:0000305|PubMed:9383199};
CC -!- ACTIVITY REGULATION: Fenoxanil inhibits arp1 scytalone dehydratase
CC activity (PubMed:19703288). {ECO:0000269|PubMed:19703288}.
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203,
CC ECO:0000269|PubMed:9383199}.
CC -!- SUBUNIT: Homotrimer (By similarity). Each subunit contains an active
CC site, located in the central part of the hydrophobic core of the
CC monomer, which functions independently (By similarity).
CC {ECO:0000250|UniProtKB:P56221}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:26972005}.
CC -!- DEVELOPMENTAL STAGE: Expressed during conidiation.
CC {ECO:0000269|PubMed:9383199}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of dihydroxynaphthalene
CC (DHN)-melanin and results in reddish-pink conidial phenotype
CC (PubMed:9383199, PubMed:26972005). Up-regulates complement component C3
CC deposition on conidial surfaces (PubMed:9383199). Causes enhanced
CC insect mortality compared to the parent strain in a wax moth Galleria
CC mellonella infection model, probably through exacerbated immune
CC response of the wax moth (PubMed:19156203).
CC {ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:26972005,
CC ECO:0000269|PubMed:9383199}.
CC -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
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DR EMBL; U95042; AAC49843.1; -; Genomic_DNA.
DR EMBL; AAHF01000001; EAL94055.1; -; Genomic_DNA.
DR RefSeq; XP_756093.1; XM_751000.1.
DR AlphaFoldDB; O14434; -.
DR SMR; O14434; -.
DR STRING; 746128.CADAFUBP00003261; -.
DR EnsemblFungi; EAL94055; EAL94055; AFUA_2G17580.
DR GeneID; 3513289; -.
DR KEGG; afm:AFUA_2G17580; -.
DR VEuPathDB; FungiDB:Afu2g17580; -.
DR eggNOG; ENOG502SNND; Eukaryota.
DR HOGENOM; CLU_101889_1_0_1; -.
DR InParanoid; O14434; -.
DR OMA; TVRWNEY; -.
DR OrthoDB; 1377897at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030411; F:scytalone dehydratase activity; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:AspGD.
DR GO; GO:0046148; P:pigment biosynthetic process; IMP:AspGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR004235; Scytalone_dehydratase.
DR Pfam; PF02982; Scytalone_dh; 1.
DR PIRSF; PIRSF024851; SCD1; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 2: Evidence at transcript level;
KW Conidiation; Endosome; Lyase; Reference proteome; Sporulation.
FT CHAIN 1..168
FT /note="Scytalone dehydratase arp1"
FT /id="PRO_0000097637"
FT ACT_SITE 84
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT ACT_SITE 109
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
SQ SEQUENCE 168 AA; 19716 MW; F40C22CEB6D02695 CRC64;
MVEKKPNLTL EFHDYLALKK VLFDWADSYD AKDWDRLRSI IAPTLTVDYR QIGLRKWDDM
PAEDYMAMIS DMDFLGDPTV KTQHLLGESW WEKISDTEVI GHHQLRAAHQ VYTDSTLQTV
KLKGHGHATN EHYYRKVDGV WKFAGLKPTV RWNEYQFEDV FRAAKPSV
