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}.
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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
//