NPS11_SERL9
ID NPS11_SERL9 Reviewed; 1099 AA.
AC F8P9P5; A0A1B1ZGC2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Adenylate-forming reductase Nps11 {ECO:0000303|PubMed:27457378};
DE EC=1.2.1.- {ECO:0000269|PubMed:27457378};
DE AltName: Full=Benzoic acid reductase {ECO:0000303|PubMed:27457378};
DE AltName: Full=Nonribosomal peptide synthase-like enzyme 11 {ECO:0000303|PubMed:27457378};
DE Short=NRPS-like {ECO:0000303|PubMed:27457378};
GN Name=nps11 {ECO:0000303|PubMed:27457378}; ORFNames=SERLADRAFT_453044;
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=S7;
RX PubMed=27457378; DOI=10.1016/j.fgb.2016.07.008;
RA Brandenburger E., Braga D., Kombrink A., Lackner G., Gressler J.,
RA Kuenzler M., Hoffmeister D.;
RT "Multi-genome analysis identifies functional and phylogenetic diversity of
RT basidiomycete adenylate-forming reductases.";
RL Fungal Genet. Biol. 112:55-63(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7.9;
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- FUNCTION: Adenylate-forming reductase, a natural product biosynthesis
CC enzyme that resembles non-ribosomal peptide synthetases, yet serves to
CC modify one substrate, rather than to condense two or more building
CC blocks. The A-domain preferentially accepts benzoic acid as substrate.
CC The natural product of the enzyme is not yet known.
CC {ECO:0000269|PubMed:27457378}.
CC -!- DOMAIN: Contains three distinct domains: an adenylation (A) domain that
CC activates the substrate amino acid which is subsequently covalently
CC linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine
CC prosthetic group of the second domain, the peptidyl carrier protein
CC (PCP) domain, as well as a reductase (R) domain of the short-chain
CC dehydrogenase/reductase (SDR) type. {ECO:0000305|PubMed:27457378}.
CC -!- SIMILARITY: Belongs to the adenylate-forming reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGO20374.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KX118591; ANX99775.1; -; mRNA.
DR EMBL; GL945441; EGO20374.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_007323119.1; XM_007323057.1.
DR AlphaFoldDB; F8P9P5; -.
DR SMR; F8P9P5; -.
DR EnsemblFungi; EGO20374; EGO20374; SERLADRAFT_453044.
DR GeneID; 18816887; -.
DR KEGG; sla:SERLADRAFT_453044; -.
DR HOGENOM; CLU_002220_1_0_1; -.
DR InParanoid; F8P9P5; -.
DR Proteomes; UP000008064; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; NADP; Nucleotide-binding; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein.
FT CHAIN 1..1099
FT /note="Adenylate-forming reductase Nps11"
FT /id="PRO_5003376645"
FT DOMAIN 578..664
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 29..360
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255"
FT REGION 717..952
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255"
FT BINDING 244
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 347..348
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 352
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 432..435
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 721..724
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 809..811
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 883
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 887
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT MOD_RES 613
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1099 AA; 119952 MW; B2E7B2F8A77BD160 CRC64;
MADPSFSYTL HYPPVDGSLL FPEIIAFNAE HNSNVPFFVF PEDGSANGVV SISHLEFYRA
CHRVAHALRP NRAGPDGEII AIIAMTDTIQ YFALLVGVII AGYIPFPMSP RNSAAAVSNL
LLKTSCHRLI TTQHSLQPLL DGIKSELGSF NFSFQDVPCL AHIYPKLGLE TIDDPFEPFP
ARPSRPSASE VMMYLHSSGS TGFPKAIPQT HQTVIHWCAA APVVDTKLYP ADTCLGVMLL
PSFHTLGIIC SLYLPLITLR SVSVYAPTSY NDPKAIPVIP TSENILEGVQ RTNCNALMAV
PAFIELWALS PSAIEILKSL RFLASSGGPL SEKVGNALAS VGVPLVNVYG GTECGGLNSM
FRRKDEVCDW VWINLSPRVM FRWVPQGEGL YECQILQSEM HRVSVENLPD VKGYATSDIF
LKHPTKEGLW KLVGRKDDII VLSSGEKTVP APMENTIASN PVVGGTVMFG RARNHVGILI
EPRQGFDVNI DDPKQVAAFR NRIWPEVEEA NKAAAAFSRI FKEMILITRP DKPLPRTGKG
TVMRKAAVTI YDKEIDALYD TVEASTTVNK DVELPKDWSE ESLVVWLGEH AARVNSDKKV
DPEVDVFEQG FDSLTATFLR NRIIGSLSSS TDSNVRTTAR QIDQNIVFSN PTIKRLSQAL
ARVVSNPQFT GKEGSLINRK VELENTLAMY SEGLPGTLSP QVEQPNGDGH SCHVVLLTGS
TGGLGSYLLA SLLENEQVSL VYAFNRSSKD GKSSEERQKA GFEDRGLDIA LLSSPKLRYI
EGDAAQDKLG LGDATYDKLR TSINVIIHNA WRLDFSLSLS SFGSNIKGTR NLVDLALSSP
NAPSLRFLFT SSISSAQGWD KSKGACPEEV LFDANVASGG SGYGASKYVC ERILEKSGLQ
ASSFRIGQIS GGQPRGAWSV TDWFPMLVKS SLALGALPVA KGVVSWLPPH AVSQAILDVA
FAKAKPPPVI NLVHPRPVQW AALMQSIGDA LVHNNLLTKP LPIVAFEEWF SRLEQKAIGA
SADDFKEMPA LKLLPFMRMI AQSDKSIRKV TSDGEAGGFV VFSTTKAQQL SRTMRELAPI
TAEDVALWMK YWASKGMFM
