ID   LYS2_CANAX              Reviewed;        1391 AA.
AC   Q12572;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 111.
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   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11651 / B792 / 171D;
RX   PubMed=9560434; DOI=10.1007/s002940050336;
RA   Suvarna K., Seah L., Bhattacherjee V., Bhattacharjee J.K.;
RT   "Molecular analysis of the LYS2 gene of Candida albicans: homology to
RT   peptide antibiotic synthetases and the regulation of the alpha-aminoadipate
RT   reductase.";
RL   Curr. Genet. 33:268-275(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; U58133; AAC02241.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12572; -.
DR   SMR; Q12572; -.
DR   VEuPathDB; FungiDB:C1_02820W_A; -.
DR   VEuPathDB; FungiDB:CAWG_01102; -.
DR   BRENDA; 1.2.1.95; 1096.
DR   UniPathway; UPA00033; UER00032.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR014397; Lys2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 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..1391
FT                   /note="L-2-aminoadipate reductase large subunit"
FT                   /id="PRO_0000193149"
FT   DOMAIN          847..927
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         884
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1391 AA;  154741 MW;  B7E641866235BCDD CRC64;
     MTDFWLNYLD NPTLSVLPHD FLKPANNKSV EGTYTFNIDN GSTDFKFGLA VFAALVYRLT
     GDEDIVIATD ESANTPEFIV RLNLTPELTF QELVSKITKE YENNISQINY KALSEVSHRI
     KEAKGLDENP GLFRLSYQHA HSNQQLNTTV EGSIRDLAIY TDGTKFTIYY NALLYSHERV
     VICGEQFAQL TTVSGDTDTV IAEVFLITDF HKKNLPDPTI DLDWSGYRGA IQEIFMDNAN
     KHPDRTCVVE TVSFLESNSK TRNFSYHKLI KLLIVVGNYL KETGIKKGDI VMIYAYRGVD
     LMIAVMGVLK AGATFSVIDP AYPPARQNIY LSVAKPKGLI GLEKAGTLDQ LVVDYISNEL
     DVVSTIPQLK VQDDGTLVGG KLEGADNDCL NDYQKFKDQP AGVIVGPDSR PTLSFTSGSE
     GIPKGVLGRH YSLAYYFPWM AKRFRLSEKD KFTILSGIAH DPIQRDMFTP LFLGAQLLVP
     TADDIGTPGK LADWMAKYGA TVTHLTLAMG QLLSAQATTA IPSLHAFFVG DILTKRDCLR
     LQSLAENVFI VNMLWSLSQT QRSVSYFEIK SRKADPTYLK NLKAVMPAGT GMHNVQLLVV
     NRNDRSQTCG VGEVGEIYVR AAGLAEGYRG LPDLNAAKFI TNWYVNPDKW IEQDEANKKS
     SETSERTWSV KPRDRMYRSG DLGRYFSDGN VECCGRADDQ VKIRGFRIEL GEIDTHLSQH
     PLVRENVTLV RRDKNEEPTL ISYIVPKDSP ELKTFFADVD FPLKKSNDPI VKGLVAYREL
     IKDIKGYLKK KLASYAIPTI IVPLVKLPLN PNGKVDKPKL PFPDTAQLAA VAKLSVSSHD
     AQAAEEENLT KLEEQIRDLW LDVLPNRPAT ISKDDSFFDL GSHSILGTRI FTYEQKLNVE
     IPLVSFKGDQ RRPRFPIGLS RYNYSRREQR CRRFLKAKTY TMRRSKELSK ELSKSALLES
     YSSLKQLPSG SVNVFVTGAT GFLGSFIVRD LLTARNKNLD IKVYAHVRAS SKEAGLQRLR
     QTGITYGIWD ENWAEKIEIV LGDLSKEKFG LDNSQWSDLT NSIDVLFTMV LCHWVYPYSQ
     LRMLNVIGTI NVFNMAGEVK LKFFSFVSST SALDTDYFVN LSDELLAQGK NGISEADDLQ
     GSAKGLGNGY GQSKWAAEYI IRRAGERGLK GCITRPGYVA GFSKTGASNT DDFLLRMLKG
     SAELGLYPDI TNNVNMVPVD HVARVVTATA LNPPSSEELT VAHVTGHPRI LFNNFLGCLK
     AYGYEINPAD YPVWTSALEK FVIEESKESA LFPLLHFVLD NLPQDTKAPE LDDSNAAKSL
     KQDSKYTGED FSAGKGVDLD QTGVYISYLI KIGFLPKPTG TGEKKLPEVE ISDESLKLIS
     GGAGARGSAA K