GenomeNet

Database: UniProt
Entry: J8QB26_SACAR
LinkDB: J8QB26_SACAR
Original site: J8QB26_SACAR 
ID   J8QB26_SACAR            Unreviewed;      1392 AA.
AC   J8QB26;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=SU7_0202 {ECO:0000313|EMBL:EJS44794.1};
OS   Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS44794.1, ECO:0000313|Proteomes:UP000006968};
RN   [1] {ECO:0000313|EMBL:EJS44794.1, ECO:0000313|Proteomes:UP000006968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-6 / AS 2.3317 / CBS 10644
RC   {ECO:0000313|Proteomes:UP000006968};
RX   PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA   Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA   Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA   Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT   "High quality de novo sequencing and assembly of the Saccharomyces
RT   arboricolus genome.";
RL   BMC Genomics 14:69-69(2013).
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:EJS44794.1}.
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; ALIE01000008; EJS44794.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000022_19_0_1; -.
DR   OrthoDB; 3305653at2759; -.
DR   UniPathway; UPA00033; UER00032.
DR   Proteomes; UP000006968; Chromosome II.
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; cd17647; A_NRPS_alphaAR; 1.
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; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 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:UP000006968}.
FT   DOMAIN          843..920
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1392 AA;  155423 MW;  EBA3B6D1B2B8AAB6 CRC64;
     MTNENTWIEK LDNPTLSVLP HDFLRPQQEP YTRPAIYSLQ VPQLDVPHDV FSNKYAAALS
     VWAALLYRMT GDDDIVLYIS NNKILRFNIQ PTWSFSELYS TISDELSQLE SIVADFSFDD
     LAEKIQNNQN LERTPHLFRL AFLENQDFKL DHFKHHLVDF TLNLETSNNA HVLNLIYNSL
     LYSSDRVTIV ADQFTQYLTA ALEDPSICIT KISLITASSK NSLPDPTKDL GWCDFVGCIH
     DIFQDNAEAF PERTCVVETP ALNSDKSRSF SYQDINRTSN IVAHYLIKTG IKRGDVVMIY
     SSRGVDLMVC VMGVLKAGAT FSVIDPAYPP ARQTIYLGVA KPRGLIVIRT AGELDQLVED
     YIKSELDIVS RINSIAIQEN GAIESGKLNE DADVLAPYEY LKDTRTGLVV GPDSNPTLSF
     TSGSEGIPKG VLGRHFSLAY YFNWMSKKFN LSENDKFTML SGIAHDPIQR DMFTPLFLGA
     QLYVPTQDDI GTPGRLAEWM SKYNCTVTHL TPAMGQLLTA QATTPFPKLH HAFFVGDILT
     KRDCLRLQTL AENCRIVNMY GTTETQRAVS YFEVKSKNDD PTFLKKLKDV MPAGKGMLNV
     QLLVVNRNDR TQICGIGEIG EIYVRAGGLA EGYRGLPDLN KEKFVNNWFV GKDYWNYLDK
     NNGEPWRQFW LGPRDRLYRT GDLGRYLPNG DCECCGRADD QVKIRGFRIE LGEIDTHISQ
     HPLVRENITL VRKNADDEPT LITFMVPRFD KPEELSKFQS DVPREVASDP MVKGLVGYHL
     LSKEIKTFLK KRLASYAMPS LIVVVDKLPL NPNGKVDKPK LQFPTPKQLN LVAENTVSEI
     DDAQFTDVER EVKDLWLDIL PTKPASVSPD DSFFDLGGHS ILATKMIFTL KKKLQIDLPL
     GTIFKYPTIK AFAAEINRIK SSGGISQEEG KATVTADYAE DAKRLVETLS KSYPSRQAFV
     EPNSSEGNTT INVFVTGVTG FLGSYILADL LKRSPKNYSF RVFVHVRAQD EKAAFGRLQK
     AGITYGTWND KFTSNIEVVL GDLSKSQFGL SDEKWTDLAN TIDVIIHNGA LVHWVYPYAK
     LRDANVISTI NVMNLAAVGK PKFFDFVSST STLDTEYYFN LSDKLVSEGK SGILESDNLI
     NSASGLTGGY GQSKWAAEYI IRRAGERGLR GCIVRPGYVT GASDNGSSNT DDFLLRFLKG
     SVQLGKIPDI RNSVNMVPVD HVARVVVATS LNPPKDNELG VAQVTGHPRI LFKDYLYTLH
     DYGYDVEVET YPEWKKSLEA SVIDRNEDNA LYPLLHMVLD DLPKGTKAPE LDDRNAVASL
     KKDIQWTSVD WSNGMGVTPE EIGIYIAFLN KVGFLPPPTH NDKFPLPSIE LTQAQISLVA
     SGAGARGSSA AA
//
DBGET integrated database retrieval system