ID A0A0F4YQF1_TALEM Unreviewed; 1425 AA.
AC A0A0F4YQF1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=T310_5456 {ECO:0000313|EMBL:KKA20512.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20512.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA20512.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20512.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KKA20512.1}.
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DR EMBL; LASV01000253; KKA20512.1; -; Genomic_DNA.
DR RefSeq; XP_013327124.1; XM_013471670.1.
DR STRING; 1408163.A0A0F4YQF1; -.
DR GeneID; 25317800; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000053958; Unassembled WGS sequence.
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 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 Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000313|EMBL:KKA20512.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 870..949
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1425 AA; 157233 MW; 567747A4855FB5E3 CRC64;
MGLNASPAQE RLERWAQRLE NLTVSPLTRD YPETNVPEAG KRPIEAFESL KLTPDALAAV
QKLSETSGSA FLVFLTAFVV LVARLTGDED IAIGTSSADD GRPFVLRVQL EASETFSQLQ
DKVEKAFTEG AADIVPLRNL RSYLQEKSKS ERAPVLFRFA AYDAPAASQE YPANTFETTD
LVINIAVSSQ STTDTHLGAY YNQRLFSSAR IGIILKQLGR LVQNAASNPN EAIGRIDFMT
EEQKAILPDP TTNLNWSRYP GAIHEIFSRN AEAHPEKLCV VETGSKTSPY REFTYRQINE
ASNLLGHYLV QSGIQRGEVV MVYAHRGVDL VVAVMGILKA GAAFSVIDPA YPPERQNIYL
DVARPRALVI IEKATQEAGE LSEQVRSFIA ENLQLRTEIP ALALRDDGSL VGGTVNGEDV
FAKQLHLKSR PVGVVVGPDS TPTLSFTSGS EGRPKGVRGR HFSLAYYFPW MAKTFHLTAD
DKFTMLSGIS HDPIQRDIFT PLFLGAQLLV PSRDDIQNEK LAEWMRKYGA TVTHLTPAMG
QILVGGATAQ FPALHHAFFV GDILIKRDCR SLQSIAPNVN IVNMYGTTET QRAVSYYEIP
SYSSQEGYLD SMKDIIPAGR GMVDVQLLVV NRFDPTRLCA IGEVGEIYVR AGGLAEGYLG
SPELNQKKFL QNWFVDPQKW VDEEKAQNQS NDEPWREFYL GPRDRLYRSG DLGRYTPTGD
VECSGRADDQ VKIRGFRIEL GEINTHLSRH PLVRENVTLV RRDKFEEQIL VSYIVPAMEK
WHAWLQERGL TDDESAEGMV GMLRRFRPLR DDVREYLRTK LPSYAVPSVI IPLKRMPLNP
NGKIDKPQLP FPDTTELSAA APRRRSSAFK ALSETEQAIA QIWAKLIPNV TTRMIGPDDS
FFDLGGHSIL AQQMFFEVRR KWRGIDISMN AIFRSPTLKG FASEIDRLIE FESFTDNQGQ
EAANGTSPAA PQLDDEYSKD ARKLVESLPA SFAAPTSSVL SDQTTVFLTG ATGFLGAHIL
RELLSRQNPS VKVVAHVRAK SEEQALDRIR SSCQAYGFWD PSWTDRLQCV RGNLGDPQLG
LSNEMWEKLS QTVDVVIHNG ALVHWVYPYA NLKPANVLGT IDALKLCASG KPKQFAFVSS
TSVLDNDHYV QESERIVAAG GAGISEADDL EGSSSGLGTG YGQSKWVGEY LVKEAGRRGL
RGTIIRPGYV TGDSTTGTTN TDDFLIRMLK GCIQLSARPN INNTVNMVPV DHVARVIIAS
AFHPPTTPLG VAQVTSHPRL RFNQFLGTLQ TYGYDVPQID YVPWARALEK YVNEGHNDKE
SQNALMPLYH FVTADLPTNT KAPELDDTNA AAALRADASW SGIDASAGSG VTEDLMGLYL
AYLVSIGFLP PPPQADTAPR KLPAITITEE QKKTLANIGG RGGAA
//
