ID T0KB12_COLGC Unreviewed; 1181 AA.
AC T0KB12;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=CGLO_07839 {ECO:0000313|EMBL:EQB52532.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52532.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB52532.1}.
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DR EMBL; AMYD01001582; EQB52532.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KB12; -.
DR STRING; 1237896.T0KB12; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_1_1; -.
DR OMA; HEIFHKN; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
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; IPR014397; Lys2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
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 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 626..704
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1181 AA; 130491 MW; 84E5CAF2491716EE CRC64;
MGLPDPTIDL DWGGYVGAIH EIFRKNALKN PDAPCVTETA SSTTIERRFT YKQIYEASNI
LANQLHEAGI TNGDVVMIFA SRCVELVIAF MGTLAAGATV TVLDPAYPPA RQQIYLEVSQ
PKALITIGRA RDDHGDFAPL VQKYMDEELS LKIQVPELRM SDDGRLTGGE IDGKQVFTDT
ESKARAPPDV LVGPDSTSIL SFTSGTTSRP KGVLGRHYSL AKYFPWMAKT FNWTSDTKFA
CLSGISHDPI QRDIFSPLFM GGELICPARE NIAHERLAEW FRDHKPNAVH LTPAMGQILC
GGAKAEFPSL KWVLYVGDIL TKKDCASLRK LAPNAEICAA YGTTETSRSV SYYHIKSRAE
DPDALDRLGD IIPAGRGIEN VQLLVVNRED PTKLCGVGES PANLRLHGYL DDEEKTKEKF
LQNWFVDNQK WVDADNKVAD HAKEPWRKYY KGPRDRIYRS GDLGYFLDDS GNAAIIGRAD
DQVKIRGFRI ELSEIDSNLR GHAIVRECKT LLRRDRNEEP TLVSYIVPEQ QEWLKWLAER
SLDDTKDEGT QIGPVFVYSK RYRPLQTEIR DHLKSRLPVQ AIPTYFIFLD KMPLNPNGKV
DSPNLPFPDA ALISQETSEE DLKRWETLSS TEKELAEQWA TLISGLNART LQPESDFFES
GGHSLLAQQL LLNIRKQLGV NMTISSLYSN SSLGALSKQI DRQRDGKNDS DAAEETEAAY
AESLDKLLGS LDAKYQAADA AALSPEGKTT VFVTGATGFL GSYIVKDLLA RESINVIAHV
RGTKSVAAAL ERLQRSLRGY GVWQDSWATR LSAVIGDLAQ PRLGLDDDTW KMLGDTVDVI
IHNGALVHWV KQYEHLERSN VLSTLDALRL CNQGKPKLFS FVSSTSVLDT DHYLDLSHEQ
TKTGQGAVME ADDMMGSRTG LGTGYGQSKW VSEQLVREAG RRGLLGSIIR PGYILGDAAT
GVCNTDDFLL RMLKGCIQLS SRPHIINTIN AVPVGHVSTV VVAASLNPIP AETANSIRSS
SDDVGVHVIH VTAHPRLRMN EYLSTLSFYG YDVPEVDYDN WKAQLETFVS AGPTQKDEQQ
SALMPLFHMA TNDLPKDTRA PELDDRNAVA VLKADADRWT GIDESAGDGI SRESVGRFLR
YLVETNFLPH PTGRGRELPA IKDGVVEAQA KWGVGGRGGA A
//
