ID   LYS2_CANAL              Reviewed;        1391 AA.
AC   Q12572;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   16-DEC-2008, entry version 53.
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   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11651 / B792 / 171D;
RX   MEDLINE=98228267; 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-
RT   aminoadipate 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-
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; U58133; AAC02241.1; -; Genomic_DNA.
DR   HSSP; P14687; 1AMU.
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:InterPro.
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:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR010071; AA_adenyl_dom.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR014397; L-NH2adipate-semiAld_DH_lsu.
DR   InterPro; IPR013120; Male_sterile_NAD-bd.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR006162; Ppantne_S.
DR   InterPro; IPR010080; Thioester_reductase.
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   1391       L-aminoadipate-semialdehyde dehydrogenase
FT                                large subunit.
FT                                /FTId=PRO_0000193149.
FT   DOMAIN      852    902       Acyl carrier.
FT   BINDING     884    884       Phosphopantetheine (covalent)
FT                                (Potential).
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
//