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Database: UniProt
Entry: A0A1V6QEF2_9EURO
LinkDB: A0A1V6QEF2_9EURO
Original site: A0A1V6QEF2_9EURO 
ID   A0A1V6QEF2_9EURO        Unreviewed;      1422 AA.
AC   A0A1V6QEF2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=PENANT_c005G01418 {ECO:0000313|EMBL:OQD87579.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD87579.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD87579.1}.
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DR   EMBL; MDYN01000005; OQD87579.1; -; Genomic_DNA.
DR   STRING; 416450.A0A1V6QEF2; -.
DR   OrthoDB; 3305653at2759; -.
DR   UniPathway; UPA00033; UER00032.
DR   Proteomes; UP000191672; 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   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; 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.
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:UP000191672}.
FT   DOMAIN          869..948
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1422 AA;  156440 MW;  FC826533E9ACAA4C CRC64;
     MAVGMASLQD RLETWAQRLN NLTVSPLTRD YPDTQKPDSK RAIEAFESLR LSKETQLQLQ
     KLSGSSSGFT VFLTAFVILV ARLTGDEDIA VGTSSEEDGR PFVIRVPIDA SETFVQLYNK
     VDKAFKEGSS QIVPLGSLRT YMQEKSKSER IPILFRFAAY DAPAASQDYP ANTFETTDLV
     VNVAPGNLSD GSAPEVELGA YYNQRLFSSV RIAFILKQLA GIARNAAANP EEAIGRIDLM
     TEDQRALLPD PTSNLNWSKF RGAIHDIFSA NAEKHPEKLC VVETQSTNSP HREFTYRQIN
     EASNILGHHL VQSGIQKGEV VMVYAYRGVD LVVAVMGILK AGATFSVIDP AYPPERQNIY
     LDVARPRALV NIAKATIDAG ELSDIVRTFI NENLELRTEI PALALLNDGT LAGGSVNGQD
     VFANEVALKS KPVGIVVGPD STPTLSFTSG SEGRPKGVRG RHFSLAYYFP WMSETFKLTP
     DEKFTMLSGI AHDPIQRDIF TPLFLGAQLL VPAREDIQNE KLAEWMQKYG ATITHLTPAM
     GQILVGGASA QFPALHHAFF VGDILIKRDC RSLQGLAPNV NIVNMYGTTE TQRAVSYFEI
     PSYSSHEGYL DTMKDVIPAG RGMLDVQMLV VNRFDPRRIC AVGEVGEIYV RAAGLAEGYL
     GSADLNAKKF LTNWFVKPEV WIEQDKAESK NEPWREFYVG PRDRLYRSGD LGRYTPSGDV
     ECSGRADDQV KIRGFRIELG EIDTHLSRHP LVRENVTLVR RDKFEEPTLV SYFVPDMSKW
     ASWLETKGLQ DDDSAEGMVG LLRRFRPLRD DAREHLRSKL PTYAVPTVII PLKRMPLNPN
     GKIDKPALPF PDTAELSAAA PRRRSSAMQA LSETELALAQ IWAKLIPNVT ARMIGADDSF
     FDIGGHSIVA QQMFFDLRRK WRGIDISMNA IFRSPTLKGF AGEIDRLLAL ESFATSDEKT
     LAGAVEAANE PDDEYSKDAR QLVDELPKSF PVRTESMLAT EPTVFLTGAT GFLGAHILRD
     LLMRKEPVTK VVALVRAKSE EQALERLRST CRAYGFWDEA WTARLQALCG DLGTPQFGLT
     QVVWDDLTNR VDAVIHNGAL VHWVYPYTTL RPANVLGTID ALKLCGSGKA KQLAFVSSTS
     ALDKDHFVEE SERIIAAGGN GISEEDDMEG SSVGLGTGYG QSKWAGEHLV REAGRRGLRG
     TIIRSGYVLG DSQTGTTNTD DFLIRMLKGC IQLNARPNIH NTVNMVPVDH VARIVIATAF
     NPPREAVNVA HVTGHPRLRF NQFLGALELY GYNVPQVDYV PWSTSLEQYV NDGQHNDKDS
     QHALMPLYHF VTADLPSNTK APELDDRNAA AALLADAAWS GIDASAGAGV TEELVGLYAS
     YLVQTGFLPA PTVAGARPLP TAQLSEEQRK TLLSIGGRGS AA
//
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