NPS9_SERL9
ID NPS9_SERL9 Reviewed; 1096 AA.
AC F8P2C8; A0A1B1ZGB1;
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 Nps9 {ECO:0000303|PubMed:27457378};
DE EC=1.2.1.- {ECO:0000269|PubMed:27457378};
DE AltName: Full=Nonribosomal peptide synthase-like enzyme 9 {ECO:0000303|PubMed:27457378};
DE Short=NRPS-like {ECO:0000303|PubMed:27457378};
DE AltName: Full=Threonine reductase {ECO:0000303|PubMed:27457378};
GN Name=nps9 {ECO:0000303|PubMed:27457378}; ORFNames=SERLADRAFT_450936;
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 L-threonine 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=EGO23306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KX118590; ANX99774.1; -; mRNA.
DR EMBL; GL945436; EGO23306.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_007320546.1; XM_007320484.1.
DR AlphaFoldDB; F8P2C8; -.
DR SMR; F8P2C8; -.
DR EnsemblFungi; EGO23306; EGO23306; SERLADRAFT_450936.
DR GeneID; 18816692; -.
DR KEGG; sla:SERLADRAFT_450936; -.
DR HOGENOM; CLU_002220_1_0_1; -.
DR InParanoid; F8P2C8; -.
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 Gene3D; 3.40.50.12780; -; 1.
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 Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00455; AMP_BINDING; 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..1096
FT /note="Adenylate-forming reductase Nps9"
FT /id="PRO_0000442638"
FT DOMAIN 569..656
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:27457378"
FT REGION 39..352
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27457378"
FT REGION 716..952
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27457378"
FT BINDING 236
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 339..340
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 344
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 425..428
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 720..723
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 807..809
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 880
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 884
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT MOD_RES 605
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1096 AA; 120372 MW; 966C6EB8E7F9E98D CRC64;
MAPGRVYPPS DKPIALLDLL HFHLVHNPYF PIYIFPNDDD TLTEISFLEF TRAVHRVAHI
VRPNRSGQDG EIVALIANTD TLLYHAIGAG MILADIVPFY MSPRNSTPAV ASMLQKTACN
RIFTIPSVHE SLISGLDGLG GPALQFQTIP TLAQVFPNLG KEKSHYPFEP YPEAAITPAL
DAVFLYLHSS GSTGYPKPIP LTNRCQLHWL QQPGILGYRH YLPDLCLGFA ALPPFHSLGN
CMQLYTPLIS VITVALYAPT SFHDPTAPPV IPTSENILDN LRKTGANCII VVPSFLEQWA
WDEKAVETLK NMSLVLYGGG PLSSKVGDAL CAAGVSLAVQ YGTTEFGAPT QLPDKVQLEN
GLWEWMRFGL SVLIRWVHQG DETYECQLLT TEKYQMAVEN MSDVKGYATS DLFVKHPTHE
GLWKIIGRTD DVLTLASGEK TVPAMMEGII SSSAHVNGVI MFGRGRNQVG VLVEPRSAHV
DLADNKAIEE FRNRIWYEVD EANKNAPTFS RIFKEMILIT SPDKPMFRVG KGTTSKNATL
KAYEEEIDAL YRTVEASTKI GNSTAPPSEW TVSTLEHWLN EQATELALGT IVVPNIDLFA
QGFDSLSATF LRNRIIGAMR SFPDLQLRAA ARRIPHNLVF ECPNIKLLAD RVAKIAGQPQ
SQVNEQVKGS ALHDAKMEIE TMLGKYSAEL RRTKKTNGSH VESSASTKAG RTVVLLTGST
GGLGSYLLAS LLKNEEVAKV YALNRHSKAS RVQQRQTAVF EDRELDVALL KLDKLIFIEA
DATAERCGLN EQTYDQLRQS VTVIIHSAWR VDFNLPLSSF EPNVRGTFQL VDLALSSTLH
STPRFLFISS VGSAQGWDRS RGAFPEDVQL DASVAVGSGY GASKYIAERL VTSSGLNATS
LRLGQIAGGP NGAWTLSDWF PILVKSSLAL GKFPNIQAYV SWMPAEKVSA AILDVALAKH
APPPALNIVH PHPVSWPDVL KPVRDAVVAK KRLPKESLPF VRMSEWVALL EMRAEEATES
DINAIPAIKL LDWFRALAGV DEDLQRTGRT DVEVGGIVKM VTEKAQSISA TLSGLSQIGQ
ADAKLWVDYW IARGLF
