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   16-JUN-2009, entry version 48.
DE   RecName: Full=L-aminoadipate-semialdehyde dehydrogenase large subunit;
DE            EC=1.2.1.31;
DE   AltName: Full=Alpha-aminoadipate reductase;
DE            Short=Alpha-AR;
GN   Name=lys2;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Penicillium;
OC   Penicillium chrysogenum complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AS-P-78;
RX   MEDLINE=99005248; 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-
CC       aminoadipate by NADPH.
CC   -!- CATALYTIC ACTIVITY: L-2-aminoadipate 6-semialdehyde + NAD(P)(+) +
CC       H(2)O = L-2-aminoadipate + NAD(P)H.
CC   -!- COFACTOR: Binds 1 phosphopantetheine covalently (Potential).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungi route): step
CC       1/3.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
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DR   EMBL; Y13967; CAA74300.1; -; Genomic_DNA.
DR   HSSP; P14687; 1AMU.
DR   BRENDA; 1.2.1.31; 285.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase a...; IEA:EC.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR014397; L-NH2adipate-semiAld_DH_lsu.
DR   InterPro; IPR013120; Male_sterile_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR006162; Ppantne_S.
DR   InterPro; IPR010080; Thioester_reductase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   TIGRFAMs; TIGR03443; alpha_am_amid; 1.
DR   TIGRFAMs; TIGR01746; Thioester-redct; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase;
KW   Phosphopantetheine.
FT   CHAIN         1   1409       L-aminoadipate-semialdehyde dehydrogenase
FT                                large subunit.
FT                                /FTId=PRO_0000193151.
FT   DOMAIN      863    934       Acyl carrier.
FT   MOD_RES     896    896       O-(pantetheine 4'-phosphoryl)serine
FT                                (Potential).
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
//