ID   A0A0G2FIM2_9PEZI        Unreviewed;      1165 AA.
AC   A0A0G2FIM2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative l-aminoadipate-semialdehyde dehydrogenase large subunit {ECO:0000313|EMBL:KKY33966.1};
GN   ORFNames=UCDDA912_g06070 {ECO:0000313|EMBL:KKY33966.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY33966.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY33966.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY33966.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY33966.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY33966.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY33966.1}.
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DR   EMBL; LCUC01000221; KKY33966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FIM2; -.
DR   STRING; 1214573.A0A0G2FIM2; -.
DR   OrthoDB; 3305653at2759; -.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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   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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
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; 2.
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   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT   DOMAIN          615..693
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1165 AA;  128605 MW;  51D9A8E1FB9712E6 CRC64;
     MGLPDPTTDL DWSGYVGAIH EIFQKNALKN PDAPCVTETA SSTTPERRFN YKQIYEASNI
     LANQLFEAGI TNGDVVMIYA YRSVELVIAF MGTLAAGATI SVLDPAYPPA RQQIYLEVSQ
     PKALVTIGRA RDENGTLAPR VQNYIDEELS LKIRIPELRM NDVGHLTGGE VDGKEVFTDT
     QSKASAPPGV LVGPDSISIL SFTSGTTSTP KGVLGRHYSL AKYFPWMAST FNWTSDTKFA
     CLSHDPIQRD IFTPIFMGGE LICPARENIA HERLAEWFRD HKPNAVHLTP AMGQILCGGA
     KAEFPSLQFV LYVGDILTKK DCAALRKLAP NAEICAAYGT TETSRSVSYY RIKSHAEDPN
     ALDKFGDIVP AGKGIENVQL LVVNREDPTK LCSVGEVGEI MLRAAGLAEI SAPFFIRWNP
     ANIRLYGYLN DPEKTKEKFI DNWFVDNQKW VEADNKIADH TNESWRKADD QIKVRGFRVE
     LNEIDSNLRG HHLVRECKTL LRRDRNEEPT LVSYIVPEDQ EWLKWLAERR LEDTEEQGTE
     IGRVVVCSKR YRPMQTEVRD HLKSRLPGYA VPTYFIFLKK MPLNPNGKID SPNLPFPDAA
     LISEEASEED LKRWETLSST EKELAEQWAT LINGLNAKTL EPESDFFESG GHSLLAQQLL
     LNIRKNMEAN LSISSLYSNA SLRALSTQID RQREGKHDSD ATEDGEAAYA QSLDKLLGSL
     DAQYQTADPA ALSPAGKTNV FVTGATGFLG SYIVRSLLER ENVHVIAHVR GTKGVPAALE
     RLLRSLRGYG VWRDSWATRL GAVIGDLTQP RLGLDDDTWK MLGDTIDVVI HNGALVHWVK
     QYKHLERSNV LSTIDALRLC NQGKPKLFSF ISSTSILDTD YYINLSHEQT STGQGAIMEA
     DDTMGSRTGL GTGYGQSKWL VREAGRRGLL GSVVRPGYIL GDAASGVCNN DDFLIRMLKG
     CIQLSSRPHI INTINAVPVG HVSTVVVAAS LNPIPAETAN SNSASADVGV HVIHVTAHPR
     LRMNEYLSIL SYYGYDVPEV DYDRWKAQLE TFVSAGSVQK DEEQSALMPL FHMAINNLPT
     TTRAPELDDC NAVAVLKADA DRWTGVDESA GEGIGREAVG RFLRYLAETN FLPWPTGRGR
     ELPAINAGVV EAQAKWGVGG RGGVA
//