ID W9Z023_9EURO Unreviewed; 1414 AA.
AC W9Z023;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=A1O1_00420 {ECO:0000313|EMBL:EXJ95300.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ95300.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ95300.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ95300.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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 -!- 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:EXJ95300.1}.
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DR EMBL; AMWN01000001; EXJ95300.1; -; Genomic_DNA.
DR RefSeq; XP_007719529.1; XM_007721339.1.
DR STRING; 1182541.W9Z023; -.
DR GeneID; 19155328; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_0_1; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000019484; 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; 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; 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:UP000019484}.
FT DOMAIN 859..937
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1414 AA; 155627 MW; 2FE31F3020E811C7 CRC64;
MASEAGGNDR LGWWVEYLKD QTLSPLTRDY PEATSENVAK RPIEAVEALS VPSSTSKALK
KLADLGSLTT VLQTVLLVLV GRLTGDEDIS IGTNAQQDGP AFVLRTSLTA SEPFAKLFTR
VRELSSQAEA NAVPLDTVQA HLKAPALFRF AAFNGSPENA SFPGSVETTD LQLTYSYSTS
YDLRLTARYN QRLFSSARIA GILAQIARFL EDVAADVNAE VGRIVFMTPE EQKLIPDPTS
DLEWSSFRGA IHDIFSANAE AHPERTCVVE TKSEDGPERK FTYQQIHESS NILAHHLVQS
GLERGDVVMI YSYRGVDLVV AVMGTLKAGG TFSVLDPAYP PDRQNVYLDV SRPRALVVIE
KATQDAGELS EKVREFIGEN LHLKTEVPAL RLGDDGTLQG GEVGGKDVFE SVRGLKAKSP
GVVVGPDSIP TLSFTSGSEG KPKGVRGRHF SLAFYFDWMA KTFNLSEKDK FTMLSGIAHD
PIQRDMFTPL FLGAQLLVPS KNDIQNERLA EWMKEHGATV THLTPAMGQI LVGGAVARFA
GLHHAFFVGD ILIKRDCKSL QNLAPNVRIV NMYGTTETQR AVSYYEIPSR NEREGYLDGM
KDVIPAGRGM YNVQMLVVNR HDRTKLCAVG EIGEIYVRAS GLAEGYLGTP ELTKKKFVDN
WFTGHEKGLE IDRARFEAKY KNEPWAKYYL GPRDRLYRSG DLGRYTPTGD VECSGRADDQ
VKIRGFRIEL GEIDTHLSQH PLVRENVTLV RRDKFEEQTL VSYVVPQLKA WTQFLSEKGL
QDEQDDGSLV GRFERFRLLQ QEVQEYLRTK LPAYAVPAII VPMRAMPLNP NGKIDKPKLP
FPDTTLLSAS RRRKSSMAHQ LTETELALAH IWAKLVPGLP PRSIKPSESF FNIGGESMKA
QQLAYQVRRT LGVDLPISKI YNRPTLKEMA AIIDHMHAAN SLEGGNEDEK PDGVTNGVKS
EDDYGADAIR MAEQLPASFP SASAEIPSSP VVFLTGATGF LGSYILKDLL DRQSPQISKV
IVLVRAKDDE TAMSRVKVTC QAYGVWADSW ASRIQGVAGS LGPARFGLSE TAWNTLIDEV
DVVIHNGAQV HWINTYEMLK PANVLGTIEA LKICAARNSR NKSKLFAFVS STSVLDHDHY
VFESERIIAA GGEGISEDDD LQASRHGLGT GYGQSKWVAE YLTREAGRRG LRGCIVRPGY
VLGSSQTGVT NTDDFLIRML KGCVQLGTRP NINNTVNMVP VDHVARTVAA CAFHPPSPHG
VAVAHVTGHP RLRFNQYLAA LQTYGYKADL VDYVPWASSL EHYVSSQQDF ALMPLFTFVA
NDLPSNTRAP ELDDRNAEKA LYEDSEWTKV DVSEGSGVTK NTVGLYLAYL VEIGFLPPPN
AVAQDGAVKR LPRVSISEEQ RKALASVGGR GGLS
//
