LYS2_CANGA
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 25-MAY-2022, entry version 120.
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; OrderedLocusNames=CAGL0K07788g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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-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; CR380957; CAG61522.1; -; Genomic_DNA.
DR RefSeq; XP_448559.1; XM_448559.1.
DR AlphaFoldDB; Q6FMI5; -.
DR SMR; Q6FMI5; -.
DR STRING; 5478.XP_448559.1; -.
DR EnsemblFungi; CAG61522; CAG61522; CAGL0K07788g.
DR GeneID; 2890361; -.
DR KEGG; cgr:CAGL0K07788g; -.
DR CGD; CAL0133971; CAGL0K07788g.
DR VEuPathDB; FungiDB:CAGL0K07788g; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_1_1; -.
DR InParanoid; Q6FMI5; -.
DR OMA; ENDKFTM; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000002428; Chromosome K.
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 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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 SMART; SM00823; PKS_PP; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..1374
FT /note="L-2-aminoadipate reductase large subunit"
FT /id="PRO_0000193150"
FT DOMAIN 828..905
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 865
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="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
