ID   N6235_COPC7             Reviewed;        1026 AA.
AC   A8NVB7; A0A1B1ZGC5;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 3.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Adenylate-forming reductase 06235 {ECO:0000303|PubMed:27457378};
DE            EC=1.2.1.- {ECO:0000269|PubMed:27457378};
DE   AltName: Full=Alanine/valine/serine reductase {ECO:0000303|PubMed:27457378};
DE   AltName: Full=Nonribosomal peptide synthase 12-like enzyme {ECO:0000303|PubMed:27457378};
DE            Short=NRPS-like {ECO:0000303|PubMed:27457378};
GN   ORFNames=CC1G_06235;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=AmutBmut;
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=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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-serine, L-alanine and L-
CC       valine as substrates. 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 ferredoxin-NADP
CC       reductase (FNR) type. {ECO:0000305|PubMed:27457378}.
CC   -!- SIMILARITY: Belongs to the adenylate-forming reductase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU85219.2; Type=Erroneous gene model prediction; Evidence={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; KX118592; ANX99776.1; -; mRNA.
DR   EMBL; AACS02000004; EAU85219.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001836648.2; XM_001836596.2.
DR   AlphaFoldDB; A8NVB7; -.
DR   SMR; A8NVB7; -.
DR   STRING; 5346.XP_001836648.2; -.
DR   EnsemblFungi; EAU85219; EAU85219; CC1G_06235.
DR   GeneID; 6013195; -.
DR   KEGG; cci:CC1G_06235; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_005562_2_0_1; -.
DR   InParanoid; A8NVB7; -.
DR   OrthoDB; 808472at2759; -.
DR   Proteomes; UP000001861; 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; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1026
FT                   /note="Adenylate-forming reductase 06235"
FT                   /id="PRO_0000442641"
FT   REGION          37..422
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27457378"
FT   REGION          556..638
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000305|PubMed:27457378"
FT   REGION          682..901
FT                   /note="Reductase (R) domain"
FT                   /evidence="ECO:0000305|PubMed:27457378"
FT   BINDING         332..333
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT   BINDING         412..415
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT   BINDING         685..688
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT   BINDING         769..771
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT   BINDING         840
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RKB1"
SQ   SEQUENCE   1026 AA;  112876 MW;  0B663347CAC17C75 CRC64;
     MGSDLLSHLS ANDRALFWEY GQGAKAFVPF QCAHHAFEFH AKANPDLTAV EEFETKITYK
     ELDRQANCLA TRLRGSGVNV GSRVCLLVER SPWLVIGVLG VLKAGAAYIP FDGNVVSDST
     LKHAIQDSAP TVILTLRKFQ HRVADAASTE IVYLDETLCT SYNPNHCTKP RDFTSSTNSV
     YIIYTSGTTG TPKGVNVTHG NVTNLLCIAP GNLGMKPGIK VSQMLNISFD FAAWEILGSM
     VNGATLCLRG KTSKEWKAVM RNVDILFSTP SMLAPHNPAD YPNLSTVVVA GEACPKATAD
     LWGARVKFYN ACGPTEVTIA NTMQLHTPGD IVTIGGPTPN NSVYVLDENM RPVPIGEPGV
     MWGGGAGITK GYLNLPDKTA ERYVPDPFAD DGSMMFNTGD LGRWHSNGTL VHLGRIDNQV
     KIKGFRVELD GVATAMETCP GVQAATALLI DGELWGFATP ASLKPEDIKE AALKVQPYYA
     VPTRYLTLDE FPETANGKTD KRILRQMALD AKNQEEKPAN KAPAQNAAWV NLPTTVIAQA
     AGAQPPTIPH RSSERSLVST VGSTVVGSQV KQVDSSASSA LEKEEYIWSG YLEDEVPEKT
     QGRIVRNLRH QIFNLYRRLF SVVFIINMAL FIWILVTKDY DAHRLGGIVV ANVFIGVLMR
     QEMVINTLFI IFTAVPPSWP LCIRRVCARI YTIGGIHSGA GVSAFVWLVA FTAQATKEMI
     NKGKTSVRTV AITYVILAEL LGILIFAYPA LRKKMHDTFE NTHRYLGWTA LALVWIQFMF
     LTIDYLPEGQ TLGQTLVKSP HFWLVIIFTI SIIWPWFRLR KVDCRPEVLS NHAVRLWFDY
     GVTPDAGTFV RLSDAPLKEW HGFASISIPG RTGYSVVVSR AGDWTSKHIN DPPTKMWVKG
     VPTYGVLKLV PMFRRMVLVA TGSGIGPCAP AILRRQIPMR VLWTAPNVRE TFGDNLCNSI
     LEACPDAVIY DTRKHGKPDM VKLVLRLVKE FDAEAVAIIS NQPLTEKVVY GCMSRGIPAF
     GAIWDS