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Database: UniProt
Entry: Q6FMI5
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Original site: Q6FMI5 
ID   LYS2_CANGA              Reviewed;        1374 AA.
AC   Q6FMI5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   26-NOV-2014, entry version 78.
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; OrderedLocusNames=CAGL0K07788g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the activation of alpha-aminoadipate by ATP-
CC       dependent adenylation and the reduction of activated alpha-
CC       aminoadipate by NADPH. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O
CC       = L-2-aminoadipate + NAD(P)H.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000305};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungal route): step
CC       1/3.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00258}.
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DR   EMBL; CR380957; CAG61522.1; -; Genomic_DNA.
DR   RefSeq; XP_448559.1; XM_448559.1.
DR   ProteinModelPortal; Q6FMI5; -.
DR   GeneID; 2890361; -.
DR   KEGG; cgr:CAGL0K07788g; -.
DR   HOGENOM; HOG000191209; -.
DR   InParanoid; Q6FMI5; -.
DR   KO; K00143; -.
DR   OMA; DRFTMLS; -.
DR   OrthoDB; EOG74TX6Z; -.
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   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
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; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 1.
DR   SUPFAM; SSF47336; SSF47336; 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; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1   1374       L-aminoadipate-semialdehyde dehydrogenase
FT                                large subunit.
FT                                /FTId=PRO_0000193150.
FT   DOMAIN      833    902       Acyl carrier. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   MOD_RES     865    865       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   1374 AA;  152537 MW;  FF8BF53926B4B184 CRC64;
     MSWKERLDNP TLSVWPHDYL RPHAEPFVEQ GTYSISIPQL SGDYATLLAA WTALLYRVTG
     DDDIVLYVRD NKVLRFTITP ELTFTQLQNK INEQLAELAN VEGTNFDALS ESLQKESGLE
     RPPQLFRIAC VTEDLQLDRY THSPLDIGLQ LHESSSDVSI VFNKLLFSQD RITILADQLT
     LFLTSVLQNA KQVFTKVSLI TDSSTSILPD PKANLDWCGF VGCIHDIFQD NAEKFPERTC
     VVETPPINST KTRTFTYKDI NEASNIVAHY LINTGIKRGD VVMIYSSRGV DLMVCVMGVL
     KAGATFSVID PAYPPARQTI YLGVAKPKGL IVIRAAGQLD QLVEDYITKE LDLVSRIPSI
     AIQDNGTVEG GSLPSESGDV LASYTELKST RTGVVVGPDS NPTLSFTSGS EGIPKGVLGR
     HFSLAYYFSW MAKQFNLSEN DKFTMLSGIA HDPIQRDMFT PLFLGAQLYV PTQDDIGTPG
     RLAEWMGKYG CTVTHLTPAM GQLLTAQAVT PFPKLHHAFF VGDILTKRDC LRLQTLAENC
     CIVNMYGTTE TQRAVSYFEV TSRSQDPHFL KKLKDVMPAG RGMKNVQLLV VNRNDRTQVC
     GVGEIGEIYV RAGGLAEGYR GLPDLNKEKF VNNWFVEEGH WNYLDKDLEA PWKEFWQGPR
     DRLYRTGDLG RYLPNGDCEC CGRADDQVKI RGFRIELGEI DTNISQHPLV RENITLVRNN
     LEGEKCLVTY MVPRFDKPEL ENFKIEVPSN ISDDPVVCGL IGYSPFTKDL KAFLKKRLAS
     YAIPSLIIVL PKLPLNPNGK VDKPKLQFPT VKQLELVAKN SSIDINDSEF NQQEREIRDL
     WLECLPTKPT SISPEDSFFD LGGHSILATK MIFTVKKQLN VELPLGTIFK YPTIKAFAAE
     VSRLKSTDKI EEETTALTAD YASDAASLID TLPKSYPAAR ALGSPSEMAG PTTVNIFVTG
     VTGFLGSFIL SDILNRTVTG VNFKIFAHVR AADETSGLDR IRKAGTVYGT WKEEYANSLQ
     VVIGDLSKKN FGLTDDKWSH LSETIDIIIH NGALVHWVYP YSKLRNANVV STINIMNLAS
     EGKPKLFNFV SSTSVLDTNH YFELSDKLQQ SGKEGIPESD DLMGSSLGLT SGYGQSKWAA
     EHIIRAAGKR GLRGSIIRPG YVTGASYNGS SNTDDFLLRF LKSAVQLGKI PDINNTVNMV
     PVDQVARVVV AASINPPCGD DLCVVHVNAH PRIIFKDYLY ELKNYGYDVE IENYEQWKKT
     LEEAVIERSE DNALFPLLHM VLGDLEDSTK APELDDKNAI TSLRADIEWT NEDRTKGMGA
     TPEQIGIYIS FLESVGFLPH PKHFGDKALP NIKISEQQKE LVASGAGARS SSAA
//
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