ID A7TQ42_VANPO Unreviewed; 1381 AA.
AC A7TQ42;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 107.
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=Kpol_1006p6 {ECO:0000313|EMBL:EDO15610.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO15610.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 ---------------------------------------------------------------------------
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; DS480452; EDO15610.1; -; Genomic_DNA.
DR RefSeq; XP_001643468.1; XM_001643418.1.
DR STRING; 436907.A7TQ42; -.
DR GeneID; 5543708; -.
DR KEGG; vpo:Kpol_1006p6; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_0_1; -.
DR InParanoid; A7TQ42; -.
DR OMA; ENDKFTM; -.
DR OrthoDB; 3305653at2759; -.
DR PhylomeDB; A7TQ42; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000000267; 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 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:UP000000267}.
FT DOMAIN 837..914
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1381 AA; 154874 MW; DE625A10138C204F CRC64;
MSEQFWIKKL DNPTLSVLPN DYLRPHSEPL SIQRTINIKV PQLDLPIENF NDTYITSLAV
WSSLILRLTG DDDILLYIQG NRVLRFNIQK DWSFQQLYNV ISNELENLPS NDSINFDDLS
ETIKILNDNN LTPPTLFKLA FLKNEQNFNL NHFKYSPIDL AINLQLSDNE ESVLEFNYNS
LLFSDKRISI LIDQFLNFIT SITSDSNQII TQIPLLTSSS KDDIPDPTTN LGWCDFVGCI
QDIFQDNAEK FPDRTCVVET PSSSQLERIF TYQQINRTSN VVAHYLISTG IKRGDVVMIY
SSRGVDLMVC VLGVLKAGAT FSVIDPAYPP ARQNVYLSVA KPRGLIVIRS AGKLDQLVED
FITNELEIVS RIPSIAIQDD GKVEGDIAND PLSKFVQLQD TRTGVIVGPD SNPTLSFTSG
SEGIPKGVLG RHFSLAYYFN WMSKQFNLSE NDNFTMLSGI AHDPIQRDMF TPLFLGARLY
VPTQDDIGTP GKLAEWMNKY NCTVTHLTPA MGQLLTAQAV TPFPKLHHAF FVGDILTKRD
CLRLQTLAEN CTIVNMYGTT ETQRAVSFFE VESRSKNPEF LKNLKDVMPA GKGMFNVQLL
VVNRNDRTQL CGVGEVGEIY VRAGGLAEGY RGLPELNKEK FVNNWLVDEH HWDYLDKGNE
PWREFWFGPR DRLYRTGDLG RYLPDGNCEC CGRADDQVKI RGFRIELGEI DTNISQHPLV
RENITLVRKN NDNESTLITF MVPRFDKQEL QNYCSHEIID STDPTVIGLV KYNLLAKSIK
EHLKKRLASY AIPTFIVVLN KLPLNPNGKV DKPKLQFPTA KQLYEVNKCG TTNVDDSSFT
ITEKQISEVW LATLPTKPSS IALDDSFFDL GGHSILATRM IFALRKAFDI ELPLGIVFKY
PTLKALANEI DIIKSSESST TDDSVVDYYK DALELVNSLP VSFHPREPFC FNLGSSSTTI
NVFLTGVTGF LGSFILSDIL NRSTRGFEFK VYAHVRASNQ QTGLERIKKA GLTYGTWKEK
FAEKLQIVIG DLSETQFGLP DSEWSKLTTT IDVIIHNGAL VHWVYPYTNL RSANVVSTIN
VINLAAHGKP KFFTFVSSTS TLDTEYYFNL SDKLVSEGKS GIMESDDLLG SSKGLSGGYG
QSKWVSEYLI RRAGERGLRG CIVRPGYVTG DSKTGSSNTD DFLLRFLKGV VQLRKIPNIE
NSVNMVPVDH VARTVVATSL NPPSSKELSV AQVTGHPRIK FYEYLFTLQA YGYDVTIESY
DEWKGSLKSS VIENNEENAL YPLLHMVLDD LPSGTRAPEL DDSNTVKSLK NDVKWTGIDV
SKGKGIDRDQ MGIYISYLIK VGFLPPPSHK GQYELPEINL TDEQISLVSS GAGARSSSAK
N
//
