ID A0A165GEV1_9APHY Unreviewed; 1427 AA.
AC A0A165GEV1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=LAESUDRAFT_721588 {ECO:0000313|EMBL:KZT10254.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10254.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT10254.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT10254.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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; KV427609; KZT10254.1; -; Genomic_DNA.
DR STRING; 1314785.A0A165GEV1; -.
DR InParanoid; A0A165GEV1; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000076871; 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:UP000076871}.
FT DOMAIN 880..957
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1427 AA; 157534 MW; 48969FB279BD134E CRC64;
MADPRVARVA SRLQNLPSIS LPTDYPRLAG NRLVEAAFSA DLSEQTCLGL LKLALYNEDE
DDEEEAVAKN QTPSPFHLLL AAFSVLLHRY TGDTDLVIGS SSASARDPLV LRISVNPDDP
FWAVVRKVQQ VEKEAEADAL PYDAIVRALG RDKGDVSDSH APLFRVRFFD EKDTPQEHFL
RSTSLTSDLT VFVSRQHDSS RSSIAPHITL RLLYNSLLFT PARMTFIVDQ LSTLLRKIAA
NPVVLVGSVP LMTPVQRAIL PDPTADLNWC DWKGAITDVF SRNARRWPER PCVIQCLPPA
SFDAPQEKRT FDYQTILHAS NILAHHLLQG GVQREEVVMV YAYRSVELVV AVMAVLKAGA
TFSVIDPAYP PSRQTIYLKV AQPRALVILK GAGKISPPVH DFISSELQIR VEVPALELLA
DGKIVGGPSA NGVDVLKAQE SLADKDPDVV LGPDSVGTLS FTSGSTGIPK GVKGRHFSLT
HFFPWMGERF GLGEHSKFTM LSGIAHDPIQ RDMFTPLFFG ARLYVPTAED IGTPGRLAEW
MDDNEVTVTH LTPAMGQLLS AQATRQIPSL RNAFFVGDVL TKRDCLRLQC LAANVRIVNM
YGTTETQRAV SYFLIPSVSE NPTFLATQKE IMPAGEGMID VQLLVVNRND KNVPCAVGEV
GEIYVRSGGL AEGYSDTEAT VKKFVTNWFA ANAPPRKDTI RDPSSDRSGP EAQFWKGIRD
RMYRSGDLGR YLPNGIVECT GRADDQVKIR GFRIELGEID LYLSQHPFIR ENVTLVRRDK
DEEKVLVSYF VPVASPSLHE FESDIPESGD EKGVVIGMRR YRKLIKDIRE HLKKKLPSYS
VPTLFVPLKR MPLNPNGKID KPALPFPDTA QSAPAEHRGP AANPTEEAIR AIWTRILPNP
PSPLPLDESF FDLGGHSILA TRLIFEIRKA FLVDAPLGLI FEKPTIGALA AAVDELRNAD
LGIAGEKTPP AVSTPTAAPQ PAVVPKKMVY SEDYETLLSK LRPSYPSVSS DYSSRPLTVF
LTGATGFLGA FILRDLLSRS ERVKKVICLV RAADAEKALQ RLRDAASGRG VWDEQWVQQG
RLEVVKGDLD QERFGLDQQT WDRVAQQADA IVHNGALVHW VYPYERLRPA NVLGTLTAMD
LAATGKAKLF VFVSSTSAID TEYYVQLSDT LSRDQDSLGG VPESDDLEGA RTSLKTGYGQ
SKWVSEKLLF EGGRRGLKGH ILRPGYVVGD SESAVTNTDD FIWRMVKGCI QLGLVPDINN
TVNMVPVDHV ARCAAIAALA PLPPPRDALT VLHVTAHPRP TFNDFLSSLA RYGFATERCE
YLLWRSQLER HVMEVQDNAL FPLLYFVLDD LPTSTKAPEL NDGNMRALLA PHMRETNRTV
DDELMGKYLA WLIQVKFLPE PTSPNAEKKL PKLANSSAAR AVGRSGI
//
