ID A0A0D0D540_9AGAM Unreviewed; 1437 AA.
AC A0A0D0D540;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-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=PAXRUDRAFT_834458 {ECO:0000313|EMBL:KIK78756.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK78756.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK78756.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK78756.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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 -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; KN826485; KIK78756.1; -; Genomic_DNA.
DR STRING; 930991.A0A0D0D540; -.
DR HOGENOM; CLU_000022_19_0_1; -.
DR InParanoid; A0A0D0D540; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000054538; 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 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; IPR006162; Ppantetheine_attach_site.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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:UP000054538}.
FT DOMAIN 890..967
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1437 AA; 157885 MW; BD6073FF9186DBA6 CRC64;
MAVQDALSRV LARLQNLPSM SLPTDYPRPT GANKLIESAH VADLSEQTSL SLLKLALHTD
HGEAAGEETQ STENRPPAFH LLLAAFTVLL HRYTGDNDIV IGSSSAAANA PLILRLAVDP
SDTFWSIVRR VQRVEKEAEV DALPYDTILR ALCKDKEDAM ENTRPIFRVR FFDETDQPRE
NFIRSTSLTS DLTIFVTRPP ATTRSSLAPH ISLRILYNSL LFTPVRISFI VDQLSVLLRK
VSANPSALIG SVPLLTNTQK ERLPGPTADL HWCDWKGAIT DVFSRNAVRW PDRPCVIQSL
TTTAPDGAQG DRTYTYGDIR RASNILAHHL LQGGVKREEV VMIYAYRSVE LVVAVMAVLK
TGATFSVIDP AYPPSRQQTY LQVAQPRGLV VLAGAGNIGP SVREFLSNNL EIRVEVPALE
FSPTGEILGG LVDGNDVLKS RNHLAETDPN VNLGPDSIGT LSFTSGSTGI PKGVKGRHYS
LTHFFPWMGN TFSLGDESKF TMLSGIAHDP IQRDIFTPLF FGARLYVPTA EDIGTPGRLA
EWMDDNKVTV THLTPAMGQL LSAQATRQIP SLCNAFFVGD VLTKRDCLRL QSLAANVRII
NMYGTTETQR AVSYFSIPPV SVDPTFLATQ KDIMPAGEGM VDVQLLVVNR TDKTVPCAVG
EVGEIYVRSG GLAEGYLDTE ASAEKFVSNW FAPSSPPWKD TILHPPQGLA GPESRHWKGI
RDRMYRSGDL GRYLPDGRVE CTGRADDQVK IRGFRIELGE IDTLMSQHPL VRENVTLVRR
DKDEEKILVS YFVPLDGQTL NGFASELSDS EEADGMKSIP KYRRLIKDIR EHLKKKLPSY
SIPSLFVPLH RMPLNPNGKI DKPALPFPDT AHAHVAHAGI KAAANGANTR TTSPTEERLC
SMWAEVLPNA PHPIPLNESF FDLGGHSILA TRVIFEIRKV FVIEAPLGLI FAKPTISGLA
TAIDALRDPD FGIARQDSNS PPATPVTVDG VQKKLAPTVI EYGQDFENLV PRLRDSYPPL
PPDFDTRALT VFLTGATGYL GAFVLRDLLQ RQERVKKVIC LVRSSSVEKG LGRLREGSSD
RGAWDEAWVT SGRLQVVTGD LGQVNFGMDK NTWSLVAAES DAVLHNGALV HWVYPYEKLR
SPNVMGTLTA VELASTTKQK LVVFVSSTSA IDTEHYVRLS DSLSQMHNAW RGIPEDDDLE
GARIGLKSGY GQSKWVSEKL LFEAGKRGLR GHIVRPGYVV GHSRTAVTNT DDFIWRMVKG
CVQLGLVPDI NNTVNMVPVD HVARCTSLAV VAPLPNATQS VLHVVANPLP TFNNLLSSLA
DYGFLTRQCE YLVWRRELEK HVMEVQDNAL FPLLHFVLDD LPSSTKAPEL NDSNTAALLR
GHEDDCPSTV SEELMGLYLA WLVGADFLPS PPSLSPRRSL PVLANDSTIK AAGRSGI
//
