ID ARP2_METMF Reviewed; 267 AA.
AC A0A0B4HVU2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Hydroxynaphthalene reductase-like protein Arp2 {ECO:0000303|PubMed:29958281};
DE EC=1.1.-.- {ECO:0000305|PubMed:29958281};
GN Name=Arp2 {ECO:0000303|PubMed:29958281}; ORFNames=MAJ_07523;
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=29958281; DOI=10.1371/journal.pgen.1007472;
RA Zeng G., Zhang P., Zhang Q., Zhao H., Li Z., Zhang X., Wang C., Yin W.B.,
RA Fang W.;
RT "Duplication of a Pks gene cluster and subsequent functional
RT diversification facilitate environmental adaptation in Metarhizium
RT species.";
RL PLoS Genet. 14:E1007472-E1007472(2018).
CC -!- FUNCTION: Hydroxynaphthalene reductase-like protein; part of the Pks2
CC gene cluster that mediates the formation of infectious structures
CC (appressoria), enabling these fungi to kill insects faster
CC (PubMed:29958281). The product of the Pks2 gene cluster is different
CC from the one of Pks1 and has still not been identified
CC (PubMed:29958281). {ECO:0000269|PubMed:29958281}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC 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; AZNE01000049; KID96467.1; -; Genomic_DNA.
DR RefSeq; XP_014575461.1; XM_014719975.1.
DR AlphaFoldDB; A0A0B4HVU2; -.
DR SMR; A0A0B4HVU2; -.
DR HOGENOM; CLU_010194_1_3_1; -.
DR OrthoDB; 5486946at2759; -.
DR Proteomes; UP000031176; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR PANTHER; PTHR43639:SF1; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE_REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..267
FT /note="Hydroxynaphthalene reductase-like protein Arp2"
FT /id="PRO_0000445816"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 166
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 25
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
SQ SEQUENCE 267 AA; 28408 MW; 3C1BED0F6F242774 CRC64;
MASSEETPRS LAGKVALVTG AGRGIGKGIA VELAKRGASV VVNYNSAEKP AQEVVDEIAK
TGSRAVAIKA DITKVPEVSR LFQEALQHFG HLDIVVSNSG TEVFKPEEEV TEEDYDRVFN
LNTRAQFFIA QHAYVHLRNG GRIVLMSSVA ANMSGIPNHA LYAGSKAAVE GFTRSFAVDA
GHRKITVNAI APGGVKTDMY DANAWHYVPN GKPGMPMEEI DKGLAAFCPL GRVAVPQDIG
RVVAFLAHPD SEWVNGQVIL LTGGSVT
//
