ID   N3009_COPC7             Reviewed;        1025 AA.
AC   A8NS27; A0A1B1ZGC6;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 3.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Adenylate-forming reductase 03009 {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_03009;
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=EAU85986.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; KX118593; ANX99777.1; -; mRNA.
DR   EMBL; AACS02000008; EAU85986.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001835921.2; XM_001835869.2.
DR   AlphaFoldDB; A8NS27; -.
DR   SMR; A8NS27; -.
DR   STRING; 5346.XP_001835921.2; -.
DR   EnsemblFungi; EAU85986; EAU85986; CC1G_03009.
DR   GeneID; 6012458; -.
DR   KEGG; cci:CC1G_03009; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_005562_2_0_1; -.
DR   InParanoid; A8NS27; -.
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..1025
FT                   /note="Adenylate-forming reductase 03009"
FT                   /id="PRO_0000442640"
FT   REGION          38..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..900
FT                   /note="Thioester reductase (TR) 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   1025 AA;  112552 MW;  32E18D88FEC564EC CRC64;
     MASSDLLSHL SATDRALFWK YGVGAEVSVP FQCVHHAFEF HAKSNPQLTA VDELGTTLSY
     GELDRRANCL ASRLRSVGVV QGSRVCMLVE RAVTLPVAVL GILKAGAAYI PLDGNIVSDS
     TLKHALVDSG STVALTLRKF EHRLEGAPVP VVFLDDAICP SYNPSHCVKP RDTTTSKDSV
     YIIYTSGTTG TPKGVHVTHG NVTNLICIEP GQLGMKPGVR VSQMLNISFD FAAWEILGSL
     ANGATLCPRG KTSKDWKAVM RSVDILFSTP SMLAPHNPVD YPNVKTVVVA GEACPKALAD
     TWGARVKFWN ACGPTEVTIA NTMQLHIPGD IVTIGGPTPN NTAYVLDENM RPVPIGQTGV
     MWGGGAGITK GYLNLPDKTS ERYVRDPFAN DGSMMFNTGD LGKWVSNGTL QHLGRIDNQV
     KIKGFRVELD GVATAMETCA GVTGATALLI DGELWGFVKP SNISPEDIKA AAHKVQPYYA
     VPSKILTMDH FPETANGKTD KRVLQQMAIE SKEEEAKLKE EKAAIPENVA WISLPPTVVT
     APKTELTIPH RPSDHSLGST NTKISAQVKE ADSSASSTSE LEKQEYIWSG YQDDDHPEKT
     QGRLVRNLRH QIFSLYRRLF SVVFIVNAAI LIWICVKKEY DANRIGGIVI ANVFIGVLMR
     QELVINTFFL IFTSIPSSWP LFIRRTAARV YHIGGIHSGA GVSSLLWLCL FTAQATKEMI
     NGGKTSVRTV AITYVILAEL LGIVIFAYPA LRKRLHDTFE NTHRFLGWSA LALVWVQFMF
     LTIDYLPEGQ MLGQTLVKTP QFWLVIILTC SVIWPWFRLR KVDVKPEVLS NHAVRLWFDY
     VTPPAGTFMR VSDAPLKEWH GFAAIPIPGR TGYSLVVSRA GDWTSKHIAN PPTKLWVKGV
     PTYGVLKLVP MFRRMVIVAT GSGIGPCAPA IFEKRIPMRV LWTAPNVRET FGDKLVDSIL
     EANPEAVIYD TRKHGKPDMV KLTLRLVKEF NAEAVAIISN QPLTEKVVYG MMSRGIPAFG
     AIWDS