ID A0A1E5RBP3_9ASCO Unreviewed; 1375 AA.
AC A0A1E5RBP3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AWRI3579_g2807 {ECO:0000313|EMBL:OEJ84312.1};
OS Hanseniaspora osmophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ84312.1, ECO:0000313|Proteomes:UP000095728};
RN [1] {ECO:0000313|Proteomes:UP000095728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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:OEJ84312.1}.
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DR EMBL; LPNM01000008; OEJ84312.1; -; Genomic_DNA.
DR STRING; 56408.A0A1E5RBP3; -.
DR InParanoid; A0A1E5RBP3; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000095728; 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 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:UP000095728}.
FT DOMAIN 845..922
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1375 AA; 152684 MW; 9D66AC706676C5FD CRC64;
MSSSILEKYA QKLDNPTLSV LPHDYLRPQS EPFIQERXYF INPPHLFLNY TDKDSLTIAT
LAVWTSLIYR LTGDDDIVLY VDKVGVIRFT IQPNLTFKEL CSLIKNEVAS TETLKFDDFD
SLSSYVQSTK DLEVAPQLFR IGFTMDELDY PLNKFKSSPF DMVVNIRAKD EALQIAYNSL
LYSKERISNL CFQFELFLAT IRKQGEDSVI TKINLITKNT TTLPDPTKNL GWCDFRGCIH
DIFQDNAEKH PNKTLVVETP QNENGKSRVF TYKDINRASN IVAHYLIDNG IKPGDVVMIY
SSRGVDLMVC VFGVLKAGAT FSVIDPAYPP ARQTIYLGVA KPRGLIVIEA AGVLDQFVED
YVTKELDVVC RIPQIAIQED GTVLGGSNKD SLEKDVLANY QSKGDTRTGV IVGPDSNPTL
SFTSGSEGIP KGVLGRHFSL AYYFDWMSQQ FNLSSNDKFT MLSGIAHDPI QRDMFTPVFL
GAQLLVPTQD DIGTPGRLAS WMAKYEATVT HLTPAMGQLL AAQATTPIPS LHHAFFVGDI
LTKRDCLRLQ TLAENVTIVN MYGTTETQRA VSFFEVKSRS EDPSFLKSLK DVMPAGKGMF
NVQLLVVNRN DRTQICGIGE VGEIYVRAGG LAEGYRGLPD LNKEKFINNW FVEPHHWDSL
DVSHNEPWRK YWFGPRDRMY RTGDLGRYLP DGNCECCGRA DDQVKIRGFR IELGEIDTHI
SQHPLVRENI TLVRKNKDNE PTLITFMVPR FDKADELQNF QTPMDESISK DPIVKGLCGY
YKLEKNIKEF LKKRLANYAM PSIIVVLDSL PLNPNGKVDK PKLQFPTQKQ LDIVAANVSS
DIDESSFTDA EKEIVSLWLE VLPNKPSSIS PQDSFFDLGG HSILATKMIF TLRKKINVDL
PLGTIFKYPT IEAFAEQVTK AKSTNSSAET SAAAPSTVDY AADAKKIANE MLLKSYAARP
DFATSTDPIN VFVTGATGFL GSYILSDLLN RKESNIKVYA HVRASDKDAG MKRLERAGTT
YGTWKPEFQA KIEVVLGDLS TLQFGKSNAE WSKLCQEIDV IIHNGALVHW VYPYSKLRDA
NVIATVNVLN MCGSGKAKFF TFVSSTSTVD TEHFFQKTDS ILESDDLQGS STGLTGGYGQ
SKWAAEYIIR RAGERGLRGC IVRPGYVTGS SVNGSCNTDD FLVRFLKGVT QLKYIPDISN
TVNMVPVDHV ARVTTASGFH PLQEFSVVQV TAHPRVQFND YLSELKQFGY NVQVESYESW
KKHLEASVVE KGEENALYPL LAMCLDDLPG GTRAPDLDDA NAVQVLSADA KWTGVDVSSG
KGATKQQIAI YIAFLNKVGF LPTAPESSKL PKITLSADQI KLVASGASAR GSAAA
//
