LYS2_PENCH
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 25-MAY-2022, entry version 104.
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 PRIDE; 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 CDD; cd05235; SDR_e1; 1.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
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 Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR TIGRFAMs; TIGR03443; alpha_am_amid; 1.
DR TIGRFAMs; TIGR01746; Thioester-redct; 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
