ID E3RLW5_PYRTT Unreviewed; 1179 AA.
AC E3RLW5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=PTT_09387 {ECO:0000313|EMBL:EFQ93280.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ93280.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ93280.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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}.
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DR EMBL; GL533912; EFQ93280.1; -; Genomic_DNA.
DR RefSeq; XP_003298620.1; XM_003298572.1.
DR AlphaFoldDB; E3RLW5; -.
DR STRING; 861557.E3RLW5; -.
DR EnsemblFungi; EFQ93280; EFQ93280; PTT_09387.
DR KEGG; pte:PTT_09387; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_1_1; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 636..717
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1179 AA; 130597 MW; FBE85183FC9E5D41 CRC64;
MASLTKGSIP DPTADLHWSD FKGPIHEIFA ANARKHPERP CVVETATSKT PERQFTYKHI
FEATAVLAHH LVQNGVQRGE VVMIFAHRGV DLVVAIMAVL AAGATFSVLD PLYPPDRQCI
YLEVSQPRAL VVIDKAIREA GPLSDQVRTY VKENLQLRTE IPALELKNDG TLVGGTKDGK
DVLDDQQQLR AELPGVLVGP DSTPTLSFTS GSEGKPKGVK GRHFSLTHYF PWMAETFGLS
ENDKFTMLSG IAHDPIQRDI FTPLFLGAQL LVPSKEDIQH EKLAEWMRKY GATVTHLTPA
MGQILVGGAS AVFPTLHHSF FVGDLLIKRD CRRLQNLAPN VRIVNMYGTT ETQRAVSYYE
LPSCTEAPEF LDSIGDVIPA GRGMKNVQLL VVNREDRNQI CKPGESGEIY VRAGGLAEEY
LGLPDLTAAK FVENWFVDQQ KWVDEDKKKV ESLGAAEPWR EFYKGPRDRL YRSGDLGHYS
EDGNVHCTGR VDSQVKIRGF RIELGEIDSH LSAHPLVREN VTLLKRDAYE EPTLVSYIVP
EMKRWYDWLE ERGAKDSDSV EDTSMVTMLK RFKYLRDDVR EHLKKKLPAY AVPSIIVPLI
RFPLNPNGKI DRPALPFPEP AHLAAAGARR PSQLGAALTP TEKTMAGIWA ELLGDRGVTA
DGISGSDSFF DLGGHSIIAQ QLFFKIRQEW KDIDVPMTTI FQYPTLRGFS SNIDQAMDPI
GLRLDTAEAI EDDPEDEAYS ADARELANQL TEFKTREPLN PKEEVHTFLT GATGFLGAYI
LRDILSRPGK VTVLVRAQDI DAAFGRVRQT CTAYGIWEES WVSRLEPLVG DLEKENFGLE
PNTWNKLVDS VDVVIHNGAL VHWVLPYSRL RGPNVISTMT ALSMCAAGKP KNFGLVSSTS
VLDTDYFVKL SDKSLAEGGT GVPEEDDLEG ARKGLGTGYG QSKWAAEYIA RQAGKKGLSG
CVIRPGYVLG DPEYGTTNTD DFLVRILKGC IQLKSRPDIT NTINMVPVTH VARVVVASSF
NPPMAPLGVA QVTSHPRITF NEFLGALEKF GYDVPLVSYP KWKQSMESYV ADRSGTKEEN
ALLPLYHFVT GDLPADTKAP ELDDKNATEA LKKDEVWTGQ DWSQGGAVTE ETVGVYVSYL
IELGFMPKPE KKGIKELVMS RLTDAMREGM KLVGGRRGV
//
