ID A0A1X7RJU6_ZYMTR Unreviewed; 1189 AA.
AC A0A1X7RJU6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ZT3D7_G2847 {ECO:0000313|EMBL:SMQ47699.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ47699.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ47699.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT853693; SMQ47699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RJU6; -.
DR STRING; 1276538.A0A1X7RJU6; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000215127; Chromosome 2.
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:UP000215127}.
FT DOMAIN 647..729
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 192..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 131388 MW; 121EBF671D47AF22 CRC64;
MAGNTKDVRP DPTSDLRWSD YRGAIHEIFA ANALKHPDRS CVVETASSTS PERKFTYKTI
NESSNILAHH LVINGVQRGE VVMVYAHRGV DLVVAVMGVL KAGATFSVID PAYPPDRQIT
YLEVAQPRAL VNIEKATIDA GQLGPTVREY ISNHLQLRTE VPALKLQDDG TIVGGSVAGG
SDVLQDQIPK KADLPGVPVG PDSTPTLSFT SGSEGRPKGV KGRHFSLAYY FPWMAERFNL
TENERFSMLS GIAHDPIQRD IFTPLFLGAS LIVPPAEDIT FDRLANWASV NAISVTHLTP
AMGQILLGST EPKIETLRNA FFVGDVLLKR DCRRLQQLAP HCRIKNMYGT TETQRAVSFY
EIPALNEDAG YLEKMGDVIP AGTGMLNVQL LVVDREKKER QCEVGEIGEI YVRAGGLAEE
YLGDPAKNAE KFVANWFVDP QRWATEDKQR VAEGGEAEPW RECYFGPRDR MYRSGDLGRY
MPDGNVECVG RADDQVKIRG FRIELGEIDT HLSQHPLIRE NVTLVKRDHN EEQILVSYYV
PDMQKWREWY SENVDQKQQQ TGAGGIRRRV SAQETMGVAE RMKIFELLTL NARQRLKEKL
PTYAVPTLFI PMLRLPLTPN GKVDKRALPF PEQADILGAS SKADDIDART ETESALAEIW
ATHLKTRNQT SDTLPRDTSF YDLGGDSIMT VQIVPKINRR WQGANIPMSV MAGGQPTLKS
VARYIDRSLN PVDLRMDAGD DHDEPQTEHY SNDLPTQIAA LPPTIASSPM RSSKDGINIL
LTGATGFLGA YILHDAFMRK TPNHVYAHVR ASSVEAGTER IRQTCTAYGL WHDWWLTEGN
LEIIIGDLER PQLGMSSSDY TRLSTDADLI IHNGARVHWL HPYSTLKAAN VLSTLECIRL
CAIGKSKRLA FISSTSALDT EHFVKQSDAR TPVSESDTLA TSAQGLGTGY GQTKWVSECL
IREACHRGLN AVIIRSGYVM GHSQSGVSNT DDFLVRMLKG CIQVRARPDV SNTINMVPVD
RVARLVNAVA FNTESGSLAH VDARPRLTFN EYLGLLEDFG FTVPLVPYAE WKAKVETYVE
TIPQTGTDEL ALLGLYHMVT GDLPSATKAP NLDDANAQSA LKADEAEAEK GTPSAVDGES
VGKYLAFLAR RGFMPLPEEE GRRKLPELVL GKEQVEALDR VGGRGGGKS
//
