ID A0A2T9YDB6_9FUNG Unreviewed; 1434 AA.
AC A0A2T9YDB6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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};
DE Flags: Fragment;
GN ORFNames=BB561_004937 {ECO:0000313|EMBL:PVU90289.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU90289.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU90289.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU90289.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(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 -!- 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:PVU90289.1}.
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DR EMBL; MBFR01000267; PVU90289.1; -; Genomic_DNA.
DR STRING; 133385.A0A2T9YDB6; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000245383; Unassembled WGS sequence.
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; IPR025110; AMP-bd_C.
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; 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; PF13193; AMP-binding_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245383}.
FT DOMAIN 903..981
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1434
FT /evidence="ECO:0000313|EMBL:PVU90289.1"
SQ SEQUENCE 1434 AA; 159662 MW; 026DB98F567A5A74 CRC64;
MGSIQAINNV GADEVSRRLE LLCKKLDSPN EILLPTDYPR PVPLKVVEAT EEFILPQNLS
MAVLQLILFN QNLSNASNTT SAHPDDVSAT PFTVLLTAFV VLLYRFTASE DIVVGTSSES
SNPLVLRLKV SPTDSFLDVM QNVKNIEREA YENQVPFEDL IKAVAQQLTD KGLAKASDAE
NAALYSLFRV RFFNAMDTTE SVLRQTISQS TDLTVFISQE STISLRQLAP SIKLRFVYNQ
VLFTKIRIQH LWEQLQKVLL AASHATTSQS ATKYNVGTMD LLSELDRNVI PNPESDMHWS
QFPGSITEIF CKNATAHPER PLITEFINKS DINSKKLISQ KIIYSYSQMY KASRIISRYL
RSNGVVTGDV VVVYAYRGAD LLISVMGVLM AGATFSVIDP AYPPARQNIY LSVAKPKAII
VLDKAGKLHP DVLNYIDNEL DIACKLDAIA LDDNGVLTSK ISDLTHVCSL VEQSTDPMDD
VVSVGPDSVG TLSFTSGSTG IPKGVQGRHF SLTHFYPWMS QEFNITNNDR FTMLSGIAHD
PIQRDIFTPI FFGAELIIPT SEDIGIPGQL AKWMSENHIT VTHLTPAMGQ LLSSNAISTI
CTLKNAFFVG DLLTRRDCTR IQSIAPNCRI VNMYGTTETQ RAVSYYSIPS LSSNPASLLS
MKEIIPAGKG MVDVQLLVVN IHDRNNICSV GEVGEIYVRS SGLAEGYLRL EDATKEKFVN
NWFSNVNLQN ELPEYQKNLK FLGPRDRLYR TGDLGRYMPD GNVECIGRID DQVKIRGFRI
ELGEINNILS LFPQLVSSVV LVRRDKNEEQ TLVAYIVPDE KEQKRTDDPS RSQLITSIRD
YLKQKLPSYS IPAVFVPMKK LPLTPNGKID KAALPYPDTP LFRTSKVQTN ENSSNSQYSN
ISKELGNTGH KLLKIWLDLL NLPASAQITK ESNFFDLGGH SILATRMVFR IRKELAEDAP
LGIVYQSPSL QEMTIAIDDL INDMKLSNPL QKISNNGSPV LIGSTVNLQG LSLKDKEHSQ
TDYATDLELL CKQIPELSNS SEFQFPIQTN SETTNSRQPK FLLTGATGFL GAYVLSSLLK
RHPRAIVYCL TRAKCKNTAM ERVKHAAKAN LVWQDSWEQN NQVIAVVGDL ALPKLGMDES
VWNQMTNEID VIVHNGALVN WVWPYEKLRS PNVLGTIEAL KLASINHIKP LVFVSSTSAL
DTPHYVRVGD SRASGVSEDD NLEGSRIGLR SGYGQSKWVS EKLLFKAKSM GYPVSIVRPG
YVIGDTKNGV TNTDDFIWRL VKGCLELRAS PEMNNVVNLC PVDYVAQVVV EAASLPISLK
HLVYHVFNKQ QFKFKDLFSL VSEYGYTLPG TEYIKWRDNL LEYTTSSTQD NALFPLLHFV
MDDLPTSTRA PELDISNTTE LMQSINVTCP DVANLMGLYL AYLAKAQFLP LPDQ
//
