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Database: UniProt
Entry: Q4WQ17_ASPFU
LinkDB: Q4WQ17_ASPFU
Original site: Q4WQ17_ASPFU 
ID   Q4WQ17_ASPFU            Unreviewed;      1425 AA.
AC   Q4WQ17;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 125.
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=AFUA_4G11240 {ECO:0000313|EMBL:EAL89667.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL89667.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL89667.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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   -!- SIMILARITY: Belongs to the NRP synthetase family.
CC       {ECO:0000256|ARBA:ARBA00029454}.
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:EAL89667.1}.
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DR   EMBL; AAHF01000005; EAL89667.1; -; Genomic_DNA.
DR   RefSeq; XP_751705.1; XM_746612.1.
DR   STRING; 330879.Q4WQ17; -.
DR   EnsemblFungi; EAL89667; EAL89667; AFUA_4G11240.
DR   GeneID; 3509068; -.
DR   KEGG; afm:AFUA_4G11240; -.
DR   VEuPathDB; FungiDB:Afu4g11240; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_19_0_1; -.
DR   InParanoid; Q4WQ17; -.
DR   OMA; ENDKFTM; -.
DR   OrthoDB; 3305653at2759; -.
DR   UniPathway; UPA00033; UER00032.
DR   Proteomes; UP000002530; Chromosome 4.
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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000313|EMBL:EAL89667.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          868..947
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1425 AA;  157178 MW;  8C618AC1DDFA21FD CRC64;
     MGVETASLQD RLERWAQRLQ NLTVSPLTRD YPENQKADLK RAIEAFESLK LPRDVHTGLQ
     KLSGPSSGFI TFLAAFVVLV ARLTGDEDIA VATSSAEDGR PFVLRVSIDQ SETFQQLYSK
     VENAFNQGAA DIVPLGSLRS YIQEKTKSER APILFRFAAY DAPASSQEYP ANTFETTDLV
     VNVANANGST SETELGAYYN QRLFSSARIA IILKQLAQIV QNASNNPGEA IGRIDFMTDD
     QRSLLPDPTS DLHWSNFRGA IHDIFAQNAE KHPDKLCVVE TKSEQSPHRE FTYRQINEAS
     NILGHHLVRA GIERGDVVMV YAYRGVDLVV AVMGILKAGA TFSVIDPAYP PERQCIYLDV
     ARPRALINIA KATKEAGELT QLVRSFIDEN LELRTEIPAL ALQDDGTLVG GSVEGQDVLA
     NQVSLKSTPV GVVVGPDSTP TLSFTSGSEG RPKGVRGRHF SLAYYFPWMS ETFKLTPNDR
     FTMLSGIAHD PIQRDIFTPL FLGAQLLVPA REDIQNEKLA EWMREYSATV THLTPAMGQI
     LVGGASAQFP ALHHAFFVGD ILIKRDCRSL QALAPNVNIV NMYGTTETQR AVSYYEIPSY
     SSQEGFLDTM KDVIPAGRGM VDVQMLVVNR FDPSRICAIG EVGEIYVRAG GLAEGYLSNE
     ELNKKKFLTN WFVDPQKWVE KDKAESQGGN EPWRQFYVGP RDRLYRSGDL GRYTPSGDVE
     CSGRADDQVK IRGFRIELGE IDTHLSRHPL VRENVTLVRR DKFEEPTLVS YFVPDMNKWP
     AWLASKGLKD DDSAEGMVGM LRRFRPLRDD AREHLRSKLP AYAVPTVFIP LKRMPLNPNG
     KIDKPALPFP DTAELSAAAP RRRSSVLQTL SETEQALAQI WANRISNVTA RMIGPDDSFF
     DLGGHSILAQ QMFFDLRRRW RGIDISMNAI FRSPTLRGFA AEIDRLVNFE SFASNANEAD
     ATADTLATSN EADDEYSKDA RKLVETLPRS FPERTEDMLV GEPTVFLTGA TGFLGAHILR
     DLLTRKSPMA RVVALVRAKS DEQALDRIRS TCRAYGFWDE SWTSRLQCVC GDLGKPRFGL
     SEALWNDLTE RVDAVIHNGA LVHWVYPYST LKPANVLGTI DALKLCASGK PKQFSFVSST
     SVLDNDHYVL ESERIIAAGG AGISEDDDLE GSSVGLGTGY GQSKWAGEYL VREAGRRGLK
     GTIVRPGYVL GDSKTGTTNT DDFLIRMMKG CIQLSARPNI HNTVNMVPVD HVARVVIAGA
     FQPPCTPIGV AQVTGHPRLR FNQFLGALQT YGYDVPQVDY VPWKMSLEHY VNDGKHDDPE
     SQHALMPLYH FVTADLPSNT KAPELDDVHA AASLRADAAW SGIDASAGAG VTEELVGLYA
     SYLVTIGFLP PPSVSTIGVR PLPKVQLSED QKKALANVGG RGGTS
//
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