ID A0A2S4PY67_9PEZI Unreviewed; 1191 AA.
AC A0A2S4PY67;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=EPUL_001357 {ECO:0000313|EMBL:POS86947.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS86947.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS86947.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS86947.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) 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:POS86947.1}.
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DR EMBL; PEDP01000220; POS86947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PY67; -.
DR STRING; 225359.A0A2S4PY67; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000237438; 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 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; 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; 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; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438}.
FT DOMAIN 632..707
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1191 AA; 133538 MW; FF6072BB70B69FC7 CRC64;
MSYLPDPTED LDWSGYVGSI QWHFSENAKK FPDRICVVET ESLKTKERVF TYKQIFEASN
ILAHYLCDSG IGHGDIVMIW AHRSVDLVVS IMGTLASGAT FSVLDPTYPP ARQKIYLEVA
QPCAMIKIGR ATDEAGQLAP VVQKFISEGL RLKTEVPALR LSDEGTLSGC DSTEEDIFST
ARAKCFFPPD VEVGPDSNPT LSFTSGSEGR PKGVLGRHYS LVKYFGWMAE RFELSSNSRF
TLLSGIAHDP VQRDIFTPLF LGAQLLVPPK EDIQHEKLAE WMSKYKPTVT HLTPAMGQIL
VGGAVAEFPS LDRAFFVGDI LTTRDCRSLQ RLAINVHIVN MYGTTETQRA VSYFEIPSRA
KNPNALDQFK ETIPAGVGMK NVQLLVVNLQ DKSKLCKVGE VGEIYVRAAG LAEGYKGIKA
MNDKKFFMNW FIDNNVWVEA DKKNDKSESW RKFYKGPRDR LYRTGDLGKY LESGDVECSG
RADDQVKIRG FRIELNEIDS NLGQHELIRD CKTLLRRDKN EEPKLVSYIV PEPRKWYDWL
KSKDLEEVDD KGIEVPQTRY FPKRYRPLQA EIRDFLKHRL PDYAIPSILV FLEKLPLNPN
GKVDKPNLPF PDITDVTERA NEEDLKRWGS LTPIQQLVAS QWAKLIRGLD PKTIKLQDDF
FDIGGHSILA QQMLLQIRRD VGANVSINAL YEFPSLEGFS SQIDKQLNST EASSTGVGTT
DYAKSLDELI KKLPSVFQAA DKENFRNIEN PTILLTGATG FLGAFIIKEI FSRRKRQFRI
VALIRNTKNP EEAFERLKKS LLGYCIWEDS WEGRISCVVG DLSKPKLGVS SETWQNLVRD
IDVIIHNGAI VHWVKSYQQM MASNVLSTFD AISLCSTGKP KIFTFVSSTS VLDTDHYISL
SDRSAASGRN ALLESDDMQG SRDKLKTGYG QTKWVSEQLV LAAGLRGLRG SIVRPGYILN
DKETGICNTD DFLIRMLKGC IQLSSRPRII NTVNVLPVNH VALLITAASL NPLPTAISPS
SITTQPSNFV KVIHATAHPR LRMNEFLSSL EYYGYTAPEV DYDVWKKDLE IFISAGGSEK
DSEQHALMPL FHFCVSDLPA TTRAPELDDR NAVNVLKLDA QYWTGIDEST GCGVSREDIG
MILAYLIEIK FIRSQCADFQ NSRLPKLAFG EHVINSRSLV GGRGAVTNTI T
//
