ID A0A0S7DS02_9EURO Unreviewed; 1423 AA.
AC A0A0S7DS02;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Alpha-aminoadipate reductase {ECO:0000256|ARBA:ARBA00032195};
DE EC=1.2.1.31 {ECO:0000256|ARBA:ARBA00013073};
DE EC=1.2.1.95 {ECO:0000256|ARBA:ARBA00012913};
DE AltName: Full=L-aminoadipate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00031335};
GN ORFNames=ALT_008582 {ECO:0000313|EMBL:GIM40095.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM40095.1};
RN [1] {ECO:0000313|EMBL:GIM40095.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM40095.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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:0000256|ARBA:ARBA00003499}.
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:0000256|ARBA:ARBA00001581};
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:0000256|ARBA:ARBA00001477};
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:0000256|ARBA:ARBA00000512};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3.
CC {ECO:0000256|ARBA:ARBA00004827}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GIM40095.1}.
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DR EMBL; BCLY01000009; GIM40095.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DS02; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_5698; -.
DR UniPathway; UPA00033; UER00032.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR001242; Condensatn.
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; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR03443; alpha_am_amid; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44845:SF1; L-2-AMINOADIPATE REDUCTASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
SQ SEQUENCE 1423 AA; 156830 MW; F913742219A9EECA CRC64;
MGVETASLQD RLERWAQRLQ NLTVSPLTRD YPENQKADLK RAIEAFESLK LPKDVHAGLQ
NLSGSSSGFI AFLTAFVLLV ARLTGDEDIA VATSSAEDGR PFVLRVSIDQ SETFQQLYSK
VENAFNQGAV DIVPLGSLRS YIQEKSKSER APILFRFAAY DAPASSQEYP ANTFETTDLV
VNVANANGST SETELGAYYN QRLFSSARIA TILKQLAQIV QNASNNPEEA VGRIDFMTED
QRSLLPDPTS DLHWSNFRGA IHDIFARNAE KHPDKLCVVE TKSEQSPHRE FTYRQINEAS
NILGHHLVQA GIERGDVVMV YAYRGVDLVV AVMGILKAGA TFSVIDPAYP PERQCIYLDV
ARPRALINIA KATKEAGELT QLVRSFIGEN LELRTEIPAL ALQDDGTLVG GSVEGQDVLA
NQVSLKSTPV GVVVGPDSTP TLSFTSGSEG RPKGVRGRHF SLAYYFPWMS ETFKLTPNDR
FTMLSGIAHD PIQRDIFTPL FLGAQLLVPA REDIQNERLA EWMREYSATV THLTPAMGQI
LVGGASAQFP ALHHAFFVGD ILIKRDCRSL QALAPNVNIV NMYGTTETQR AVSYYEIPSY
SSQEGYLDTM KDVIPAGRGM VDVQMLVVNR FDPSRICAIG EVGEIYVRAG GLAEGYLSNE
ELNKKKFLTN WFVDPQTWVE KDKAESQGAN EPWRQFYVGP RDRLYRSGDL GRYTPSGDVE
CSGRADDQVK IRGFRIELGE IDTHLSRHPL VRENVTLVRR DKFEEPTLVS YFVPDMSKWS
SWLASKGLED DDSAEGMVGM LRRFRPLRDD AREHLRSKLP AYAVPTVFIP LKRMPLNPNG
KIDKPALPFP DTAELSAAAP RRRSSVLQTL SETEQVLAQI WANRLSNVTA RMIGPDDSFF
DLGGHSILAQ QMFFDLRRRW RGVDISMNAI FRSPTLRGFA AEIDRMVNFE SFASNANEAD
ATADTLATSN EADDEYSKDA RKLVETLPES FPERTEDMLS GEPTVFLTGA TGFLGAHILR
DLLTRKSPMA RVVALVRGKS DEQALDRIRS TCRAYGFWDE SWTSRLQCVC GDLGKPRFGL
SEALWNDLTE RVDAVIHNGA LVHWVYPYST LKPANVLGTI DALKLCASGK PKQFSFVSST
SVLDNDHYVL ESERIIAAGG AGISEEDDLE GSSVGLGTGY GQSKWAGEYL VREAGRRGLK
GTIVRPGYVL GDSKTGTTNT DDFLIRMMKG CIQLSARPNI HNTVNMVPVD HVARVVIAGA
FQPPCTPIGV AQVTGHPRLR FNQFLGALQT YGYDVPQVDY VPWKMSLEHY VNDGKHDDPE
SQHALMPLYH FVTADLPSNT KAPELDDVHA AASLRADAAW SGIDASAGAG VTEELVGLYA
SYLVTIGFLP PPSASGARPL PEVQLGEDQK KALANVGGRG GTS
//
