ID   LYS2_PENCH              Reviewed;        1409 AA.
AC   O74298;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   13-SEP-2023, entry version 110.
DE   RecName: Full=L-2-aminoadipate reductase large subunit;
DE            EC=1.2.1.31 {ECO:0000250|UniProtKB:P07702};
DE            EC=1.2.1.95 {ECO:0000250|UniProtKB:P07702};
DE   AltName: Full=Alpha-aminoadipate reductase;
DE            Short=Alpha-AR;
DE   AltName: Full=L-aminoadipate-semialdehyde dehydrogenase;
GN   Name=lys2;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AS-P-78;
RX   PubMed=9790587; DOI=10.1007/s004380050847;
RA   Casqueiro J., Gutierrez S., Banuelos O., Fierro F., Velasco J.,
RA   Martin J.F.;
RT   "Characterization of the lys2 gene of Penicillium chrysogenum encoding
RT   alpha-aminoadipic acid reductase.";
RL   Mol. Gen. Genet. 259:549-556(1998).
CC   -!- FUNCTION: Catalyzes the activation of alpha-aminoadipate by ATP-
CC       dependent adenylation and the reduction of activated alpha-aminoadipate
CC       by NADPH. The activated alpha-aminoadipate is bound to the
CC       phosphopantheinyl group of the enzyme itself before it is reduced to
CC       (S)-2-amino-6-oxohexanoate. {ECO:0000250|UniProtKB:P07702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + H2O + NADP(+) = 2 H(+) + L-2-
CC         aminoadipate + NADPH; Xref=Rhea:RHEA:12304, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58321,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-
CC         aminoadipate + NADH; Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP(+) = ATP
CC         + H(+) + L-2-aminoadipate + NADPH; Xref=Rhea:RHEA:46936,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58672, ChEBI:CHEBI:456215; EC=1.2.1.95;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250|UniProtKB:P07702};
CC       Note=Binds 1 phosphopantetheine covalently.
CC       {ECO:0000250|UniProtKB:P07702};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; Y13967; CAA74300.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74298; -.
DR   SMR; O74298; -.
DR   UniPathway; UPA00033; UER00032.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd17647; A_NRPS_alphaAR; 1.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR014397; Lys2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR03443; alpha_am_amid; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44845:SF1; L-2-AMINOADIPATE REDUCTASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase;
KW   Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..1409
FT                   /note="L-2-aminoadipate reductase large subunit"
FT                   /id="PRO_0000193151"
FT   DOMAIN          858..937
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         896
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1409 AA;  154842 MW;  A85DFD397BAB29AE CRC64;
     MAVGTASLQD RLETWAQRLK NLTVSPLTRD YPDTQKTDSK RVIEAFESLQ LPKAKLTGSS
     SSFIAFLTAF IILVARLTGD EDIAVGTNSN EDGRAFVIRV PIDTSESFAQ LYAKVDKAYK
     EGSSQIVPLG SLRSYIQEKS KSERTPVLFR FAAYDAPASS QDYPANTFDT TDLVVNVAPG
     SAEVELGAYY NQRLFSSARI AFILKQLASI ASNAAANPDE AIGRIDLMTE DQRALLPDPT
     CNLNWSNFRG AIHDIFTANA ERHPEKLCVV ETQSSSSPHR EFTYRQINEA SNILGHHLVR
     SGIQRGEVVM VYAYRGVDLV VAVMGILKAG ATFSVIDPAY PPERQNIYLD VARPRALVNI
     AKATKDAGEL SDIVRTFIDE NLELRTEIPA LALLDDGTLA GGSINGQDVF ANDVALKSKP
     TGVVVGPDSI PTLSFTSGSE GRPKGVRGRH FSLAYYFPWM SETFKLTPDE KFTMLSGIAH
     DPIQRDIFTP LFLGAQLLVP AREDIQNEKL AEWIEKYGAT ITHLTPAMGQ ILVGGASAQF
     PALHHAFFVG DILIKRDCRS LQGLAPNVSI VNMYGTTETQ RAVSYYEIPS YASNEGYLNN
     MKDVIMAGRG MLDVQMLVVN RYDPTRLCAI GEVGEIYVRA GGLAEGYLGS PELSAKKFLN
     NWFVNPEIWA EKDQAESRNE PWRQFYVGPR DRLYRSGDLG RYTPSGDVEC SGRADDQVKI
     RGFRIELGEI DTHLSQHPLV RENVTLVRRD KDEEPTLVSY FVPDMNKWAS WLESKGLKDD
     DSDSEGMVGL LRRFRPLRDD AREHLRTKLP TYAVPTVIIP LKRMPLNPNG KIDKPALPFP
     DTAELSAAAP RRASSALQAL SETEQTLAQV WAKLIPNVTS RMIGPDDSFF DLGGHSILAQ
     QMFFELRRKW RVIDISMNAI FRSPTLKGFA SEIDRLLAME SFATSDDKTL AVQAANEPDD
     EYSKDAVQLV NELPKTFPQR TEAMLTSEPT VFLTGATGFL GAHILRDLLT RKSPSTKVVA
     LVRAKTEELA LERLRSTCRA YGFWDEAWTA KLQAVCGDLG KPQFGLSQSV WDDLTNRVDA
     VIHNGALVHW VYPYATLRPA NVMGTIDALK LCASGKAKQF AFVSSTSALD KDRYVQESER
     IIAAGGNGIS EDDDMEGSRV GLGTGYGQSK WAGEYLVKEA GRRGLRGTIV RSGYVLGDSV
     TGTTNTDDFL IRMLKGCIQI GLRPNIFNTV NMVPVDHVAR IVIATAFHPP ATGVNVAHVT
     GHPRLRFNQF LGALELYGYN VPQVDYVPWS TSLEQYVNDG EHNDKESQHA LMPLYHFVTS
     DLPSNTKAPE LDDVNAATAL RADATWSGVD ASAGAGVTEE LVGLYASYLV QTGFLPAPTV
     AGARPLPAAQ ISEEQKKTLL SVGGRGGTS
//