ID A0A066X6X1_COLSU Unreviewed; 1154 AA.
AC A0A066X6X1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=CSUB01_06751 {ECO:0000313|EMBL:KDN63429.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN63429.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN63429.1}.
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DR EMBL; JMSE01001227; KDN63429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X6X1; -.
DR STRING; 1173701.A0A066X6X1; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_1_1; -.
DR OMA; ENDKFTM; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000027238; 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; 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; IPR009081; PP-bd_ACP.
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 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 623..702
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1154 AA; 127246 MW; 4CFA0F1AA6DBC3D7 CRC64;
MAPELPDPTS DLHWSAFRGA IQDIFSQNAK QYPDRLCVVE TASSTSPRRE FTYRQIDEAS
NLLANHLVAS GVQRGDVVMS YSHRGVDLVV AVFGILKAGA TFSVIDPSYP PDRQNIYLDV
ARPRALVVID KATKEAGKLT DKVRTFIAEN LDIKTEVPAL ELRADGSLVG GQVGGKDIFA
GLEKENGPNV LVGPDSNPTL SFTSGSEGKP KGVLGRHYSL AYYFDWMAER FNLSEKDKFT
MLSGIAHDPI QRDIFTPMFL GAQLLVPSKE DIQHEKLAEW MREYGATVTH LTPAMGNVLV
SNASAEFPAL HHAFFVGDIL IKRDCKALQK LAGNCYIVNM YGTTETQRAV SYYELPSASA
DPTFLQRFPD NVIPAGKGMK DVQLIVVDRE NTERVCNVGE VGEIYVRAAG LAEGYLANDE
LNKAKFVSNW FVKDNRWAEL DQQASKNEPW REFYKGPRDR MYRSGDLGKY TEDGNVVCVG
RADDQVKIRG FRIELGEIDK YLSDHPMILD NVTLVRRNKD EEKTLVSYIV PDMQRWSEWV
VQNGKKDDTS GGDSLMGRLR RFWPLGEEVR KYLKTKLPIY AIPEIIIPLE KFPLNPNGKK
DKPALPFPDA AQLAEARPHT EASDLTETER RVAGIWGSLL ANIDERSLGH DDSFFDIGGH
SILAQQMLFQ VNRTWPGVDV TMAVVFRSPS LKAFSAEIDG KLSGEAPEKV NATLEGEDYF
EDAKKLLATL PEKFTPFDKK AADVKTVFLT GATGFLGAYI LRDLLTRNAP NVRVIAHVRA
IDDIDAYNRV VKSCQAYGVW QPSWKNSLTA VQGSLGKPLL GLSQERWNSL ANEVNVIIHN
GAQVHWVLPY SNLKPANVQG TLDVISLCAT GKPKQLAFVS STSVLDHPHF VKLSQGGSLV
SEEDDLSGSS KNLGNGYGST KWVAEYLVRN AGKRGLSGTI VRPGYITGEQ YSGTSNTDDF
LLRMLKGCIQ LNSRPKIENT INMVPVDHVA RLVVASALHP PRQPLGVAQV TSHPRLTFRT
YLSALEKYGY NVPEVEYSQW SKSLQDYVAE GKEHALMGLY HLATTDLPAD SIAPELDDVN
AAAALRSDAE LTGEDLSAGG AVTDETIGRY LSYLIAIGFL EAPEKPGQLA IPPAEISPEQ
KEALLRVGGR GALV
//