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 01-MAY-2013, entry version 70.
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 mitosporic Nakaseomyces.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O
CC = 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 (fungal 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; 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 KO; K00143; -.
DR OMA; IDTHLSR; -.
DR OrthoDB; EOG4BCHW2; -.
DR UniPathway; UPA00033; UER00032.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; 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_dom.
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 SUPFAM; SSF47336; ACP_like; 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.
FT CHAIN 1 1374 L-aminoadipate-semialdehyde dehydrogenase
FT large subunit.
FT /FTId=PRO_0000193150.
FT DOMAIN 833 902 Acyl carrier.
FT MOD_RES 865 865 O-(pantetheine 4'-phosphoryl)serine
FT (Potential).
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
//
