ID A0A401GZ53_9APHY Unreviewed; 1803 AA.
AC A0A401GZ53;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SCP_1101190 {ECO:0000313|EMBL:GBE87443.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE87443.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE87443.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
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 -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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:GBE87443.1}.
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DR EMBL; BFAD01000011; GBE87443.1; -; Genomic_DNA.
DR STRING; 139825.A0A401GZ53; -.
DR InParanoid; A0A401GZ53; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000287166; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; IPR001242; Condensatn.
DR InterPro; IPR045340; DUF6533.
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; PF00668; Condensation; 1.
DR Pfam; PF20151; DUF6533; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 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 Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000287166};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1508..1531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1543..1564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1576..1597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1621..1643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1664..1684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 884..961
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 860..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1803 AA; 200369 MW; E85CD001A5BB7F1E CRC64;
MGDECLRRVV ARLQNLPSIS LPTDYPRPTG GSRLVEAAIT ADLSEQTCLG LLKLALYNED
EDGDGDGDDE KGHKTPSAFH LLLAAFSVLL HRYTGDTDLV IGSSAASARD PLVLRLEVNP
SDPFWQVVRK VQQVEKDAEV DALPFESIVR ALGKGKTDSV ESSRPLFRVR FFDETDTPQE
NFLRTTSLTS DLTVFITRQH ENSRTSLTPH ISLRILYNSL LFTPTRITYI VDQLSVLLRK
VAANPLAPVG SAPLLTSAQR AKLPNPIADL NWCGWKGAIP DVFSRNARQW PDRPCVIQCL
YPASSNESQE KRTYTYSMVL HASNTLAHHL LEGGVQREDV VMVYAYRSVE LVVAVMAVLK
AGATFSVIDP AYPSSRQKIY LEVAQPRALV VLKGAGTISP PVREFITNEL KICVEVPALE
LLTDGTITGG SRSDGGDVLK GQAHLAETDP DVPLGPDSVG TLSFTSGSTG IPKGVRGRHF
SLTHFFPWMG ERFELNKDSK FTMLSGIAHD PIQRDMFTPL FFGASLYVPT AEDIGTPGRL
AEWMADNAVT VTHLTPAMGQ LLSAQATHQI PSLRNAFLVG DVLTKRDCLR LQSLAANVRI
INMYGTTETQ RAVSYFLIPS VAEDATFLTT QKDIMPAGEG MIDVQLLVVN RNDKNIPCAV
GEIGEIYVRS GGLAEGYSDP SATAEKFVKN WFSENAPPWK DTIREPANGQ SGPEARFWKG
VRDRMYRSGD LGRYLPNGIV ECTGRADDQV KIRGFRIELG EIDTHLSQHP LVRENVTLVR
RDKDEEKVLV SYFVPVSGPL LDDFASDIPE GEDEKGLITG MHRYRRLIKN IREYLKKKLP
SYSVPTLFVP LKRMPLNPNG KIDKPALPFP DTAQAAATES QRGPTATPTE EAVRAIWTRI
LPNPPSPIPL DENFFDVGGH SILATRLIFE IRKAFLVDAP LGLVFDRPTI GGLAAAVDDI
RNADLGFTTG KTPGTLTPAT HAAVGTVKTI AYGQDYDNLL SKLRPSYSPL PADFGGKRLT
VFLTGATGFL GAFILRDLLL REDRVKKVIC LVRAPDLQKA LDRLRDAADG RGVWDEEWLK
TSRVEVVKGD LDQEFFGIEK ATWDRIADEA DAVIHNGALV HWVYPYEKLR YANVLGTLIA
VDLAATGKPK AFVFVSSTSD IDTEYYVQLS ESSHDQSSLG GVPESDDLEG ARTSLKTGYG
QSKWVSEKLL FEAGRRGLRG HIVRPGYVVG DSRTAVTNTD DFIWRLVKGC IQLGLVPDIN
NTVNMVPVDH VARCTVLAVL APLPAPRDAL SVLHIAAHPQ PTFNDMFSAL ARYGFATKRC
EYLLWRSQLE KHVMEVQDNA LFPLLHFVLD DLPTSTKAPE LNDENMRALL APHMQLTNRT
VDKELMGKFA MACERLRGKS GRPQWTVDAE NSMLLIVHMT EDKGDRVDIG LPDSANPQFY
IPRFRLDMMV DVVPTIRSVY DSDPDWLTDA SSSYLRIAAI SIAAYDYLLT LPAELRFYKV
QRSWMPSLGC ILFILIRYVS MITVTVSAIG FFASFSPQSC QRWFMVTPVF KVLQMVLSQI
IMGIRTVNIS RRKPWVVWTM LVVFLVVTCL EFFTNLYDRN YVQDRHNNCT GGDNSAHLSV
WLFYVVAMFY DVVTIGISTY FLVSFSPSSG RLSRLVRLML YDDIGYLVLL TAANVLNLVL
YRTSDGTTQS SGACLSFAVV WIMSQRILIH LREHTRTTTQ VISRPLQSPR DISDAMRSQF
ETKDQLDEEF GLPHPRAASS VQLDSVREGC ELDVQVHVEE TVTVEYAEDT SERESYRTPR
PMP
//
