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
//