NPS10_HETAN
ID NPS10_HETAN Reviewed; 1088 AA.
AC A0A1B1ZGB5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Adenylate-forming reductase Nps10;
DE EC=1.2.1.- {ECO:0000269|PubMed:27457378};
DE AltName: Full=Nonribosomal peptide synthase-like enzyme 10 {ECO:0000303|PubMed:27457378};
DE Short=NRPS-like {ECO:0000303|PubMed:27457378};
DE AltName: Full=Phenylpyruvate reductase {ECO:0000303|PubMed:27457378};
GN Name=nps10 {ECO:0000303|PubMed:27457378};
OS Heterobasidion annosum (Root rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Heterobasidion;
OC Heterobasidion annosum species complex.
OX NCBI_TaxID=13563;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=JMRC 9984;
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).
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 phenylpyruvic acid and
CC benzoic acid as substrate. The natural product of the enzyme is not yet
CC known. {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}.
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DR EMBL; KX118589; ANX99773.1; -; mRNA.
DR AlphaFoldDB; A0A1B1ZGB5; -.
DR SMR; A0A1B1ZGB5; -.
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; 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; SSF47336; SSF47336; 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..1088
FT /note="Adenylate-forming reductase Nps10"
FT /id="PRO_0000442639"
FT DOMAIN 586..668
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:27457378"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..451
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27457378"
FT REGION 712..951
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27457378"
FT BINDING 261
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 357..358
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 362
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 443..446
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 716..719
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 804..806
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 875
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 879
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT MOD_RES 621
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1088 AA; 118844 MW; A4FF5780077D4BFD CRC64;
MSSVSIQIPL PTPPPTQAHN SQTFCAPPLG SLTLPEVFDW HSKNSPNHPL YSYINIDGSI
RTITWAESVR AVHRAARRMR TELGLSSDSV PDLTAGKPVV GILAVLDSIT YSTLVTGVQY
AGFTPFPISP RNSHAAVVHL INKAFVSHII VEESCRGLLE DAFQSLKSDL TSPSMPTTSV
APVFEDLYVS SDSAQGEASV AFETPAWDSN AIIIHSSGST AFPKPIAWTH GRAMQLSTVP
WYGERDLTGK RMACHAMPMY HTMGYLLLAW AASSGLVLNG FRPQSPATKS TIENVFSASL
EAHSDIIFTV PSFVEAWSKN PAYVKTLAEL DGVMFGGGPL GKQVGDVLVS ANVTLFNLYG
STEAGVLSST VPADFNIDWE YFRISDIAKV AFVPNEENKL ELVVLSSNLN TPSVFNAVYE
DVPAYATSDL FEPHPTKPGY WKIFGRTDDQ IMHSTGEKTN PGPLEHILNQ DPHVRASLMF
GRGQFQAGVL VDPTSEYRFD PSDEEKLAEF RNLIWPSVEE MNAYAPQHSR VFKEMILVSS
PSKPFTFTAK NSVRRQAVIQ EYDDEIKAIY FAVDETGRAD IPSPTAWDSA KTLGFIRAVV
QKVMKKEVQD GDDFFQHGCD SLQATWIRNT ILRSLKDSTD ANTQDISNSF IYQHPSVASL
ASFVSSVAQG QNNINSGLDR AQEMNIMVAR YSKDFPPHVP SAPQPSKDTI LLTGSTGALG
SNILALLIAS PSVARIYAFN RKSRSSIPLL DRQKSALLER GLDPSLAASK KVVLVEGDVT
KQDLGISTEL LSEIRVSITH IIHNAWPVNF NLSLESFEPQ VKGLRHLVDL SLSSPHPSPP
RVLFTASIGM FNDITRAEPV KEVPIGANVA VSNGYGESKW VGETILAEAA KQTPLRSTSI
RVGQLSGGIN GAWTTAEWLP SLVRSAIHLK ALPDCEGDVS WIPVNVAAAA IVDFCQSDSS
IMNLVHPRPA TWSSIFSAFA SVLNIPLVPY TEWLALLRKS AEDAGDAPDA DSLQQNPGLR
LLDWYHSAFV HENDSAYQYA DTMGFPKFDM TNSLRASGTL ADEGLPQLGE SDVKLWVDYW
KKVGFFPA
