ID A0A165TF71_9APHY Unreviewed; 1044 AA.
AC A0A165TF71;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=L-aminoadipate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KZT73346.1};
GN ORFNames=DAEQUDRAFT_662515 {ECO:0000313|EMBL:KZT73346.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT73346.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT73346.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT73346.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429037; KZT73346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165TF71; -.
DR STRING; 1314783.A0A165TF71; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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 InterPro; IPR036736; ACP-like_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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 551..629
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1044 AA; 114218 MW; 28D0942FDE0795FA CRC64;
MPAPTYIASS LTDLVAIRAR DKPNDVAIYT GIDEPGPLLK PLTYSQVQRA VDRLCAHYAG
LGLTPPGKDG IPPQQVIAIL TSTAVDESLL EIALAKLGLT SLLISVNNSV PAIAHLCKIT
NSSHLIYGSK FVSEAHEAQN ILAEQDIEIE IVPDKRYPIW GPGGVDDVKI DPFTAVLSPQ
DERDRMCVIL HSSGSTGFPK PVYISHFSMI ANIAGFVNKA GFSALPVFHG FGHYSVFRCY
YAGVPFVLFP AHLPLTSTNI CKVINAIPVP CPLCFAVPYV IKLLGETEEG VRALANFESI
TFAGAAVPDD LGDRLTAAGV NIKAIYGTTE TGSLLSSERD FAADKAWNWL RMEGRIADYL
VMEDRGSGTY ESVVKDGWPA KNQSNRPDGS YATKDLFARH PQRSNWYKYI GRLDDTLVQV
LGEKTNPVPI ELAIQGNSPY VEQCIVFGAG QPQIGCLLLP SEQAKDLYKD RNAYMEKVWP
VVEDANTQAP THSRILPEMV EILEYGTQIP QATKLSFLRP ACYAKFKSII DAVYDRFENG
TSADKLDLSQ PELEDFIFNA ITHTLGATKA AKLTKTSDLF AFGVDSLQAT RIRNVCQKEL
ELNGPTLGQN VVYENPSVEK LAAYITALRS GAGQTKSVEE NHAAMWAMVD KWASKFVRRE
ATDSEQIVPP SSPGSQTIVL TGATGSLGAH ILYQLVSSPT VDRVICLSRA KSNEDSGTRL
QDSLKLRQLR LSEEQWKRIE SYAADVNEDR LGLSSAEYEG ILSRTTAVIH NAWPVNFNMN
LDSYDAHVGG ALNLMNLCLR SPKPQLPSFY FSSSIAAVTG SSDPVCNEDF PASAATALPT
GYGRSKWVIE KLAERAARAT PVHVGILRIG QLVGDTESGV WNETESWPLM FKATETTGAL
PTFQQNPQWL PVNIAGRAIA EIATHSVPPK AAVYHIVNPN MSGGWDAIIA GLKRAGMTFD
VVSRSEWLDR LARSDPDGER NPAIKLLPYY RTRFGKPTES IPMQFRVDTT CSIALSLANS
PPISQDLVEK WVQHWREVGF LGRA
//
