ID B0D6R6_LACBS Unreviewed; 1420 AA.
AC B0D6R6;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 97.
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 Name=LbLYS1 {ECO:0000313|EMBL:EDR09269.1};
GN ORFNames=LACBIDRAFT_184376 {ECO:0000313|EMBL:EDR09269.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR09269.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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 -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; DS547099; EDR09269.1; -; Genomic_DNA.
DR RefSeq; XP_001879618.1; XM_001879583.1.
DR SMR; B0D6R6; -.
DR STRING; 486041.B0D6R6; -.
DR GeneID; 6075487; -.
DR KEGG; lbc:LACBIDRAFT_184376; -.
DR HOGENOM; CLU_000022_19_0_1; -.
DR InParanoid; B0D6R6; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000001194; 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; 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; IPR001242; Condensatn.
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; PF00668; Condensation; 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:UP000001194}.
FT DOMAIN 878..955
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1420 AA; 155685 MW; 739FC589D97EE7DE CRC64;
MEDNRLARVL ARLQSLPSIS LPTDYPRPTG SNKLVEAVHL TQLSEQTSLS LLKLVLYTED
EDEDEDEVES GVKRPSAFHL LLAAFTVLLH RYTGDTDIVI GSSSAAVREP LVLRLSVDPM
DPYWAIVRRV QQIESEAESD AVPFDVLTRA LSKGKDEGIE GPLFRVRFFD ETDEPKDNFI
RSTSLSSDLT IFITRPPTST RASIAPRISL RILYNSLLFT SARITCIVDQ LSVLLRKVAS
SPLAPVGAVP LLTPTQKAKL PVPTADLNWC DWKGAITDVF SQNARRWPER PCVVQYLPPE
SLNDPQKSIT FSYDAILRAS NVLSHHLIKS GVQREEVVMV YAHRSVDLVV AVMAVLKAGA
TFSVIDPAYP ASRQIIYLRV AQPRGLVVLK GAGTISPSAR EFLSEELHIR VEVPALEVFP
DGSITGGIDA DGQDILSVHA HLGHIDPNVA LGPDSVGTLS FTSGSTGIPK GVRGRHFSLT
HFFPWMGERF GLNENSKFTM LSGIAHDPIQ RDMFTPLFFG AQLRVPTSED IGTPGRLAEW
MANSEVTVTH LTPAMGQLLS AQATRQIPSL LNAFFVGDVL TKRDCLRLQS LAANVRIINM
YGTTETQRAV SYFAIPPVSE DSTFLATQKD IMPAGEGMID VQLLVVNRND RNVPCAIGEV
GEIYVRSGGL AEGYLDQDAT AEKFVTNWFS ADSAPRKDTI LHPVDELAGS EALYWKGIRD
RMYRSGDLGR YQPDGIVECT GRADDQVKIR GFRIELGEID IHLSQHPLVR ENVTLVRRDK
DEEKILVSYF VPLEGPDLDG FASDIPDDEG TIVRGMKKYR RLIKDIREHL KKKLPSYSVP
TLFVPLKRMP LNPNGKIDKP ALPFPDTAQA SYAAPPTRKA STTEETMCSL WANILPNAPK
PIPLDESFFD LGGHSILATR LIFEIRKVFV VSAPLGLIFE QPTISGLVNA VDALRNADLG
LEAQPPVEIV PGTPAVETKA LPLEYGQDYV QLLDKLQPSY PSIPADFGER PVTVFLTGAT
GFLGAFVLKD LLSRIGRVQK VICLVRASSA ESGLDRLKEG STNRGVWDDA WVSSGRLEVV
VGDLALSQLG LGKDDWDRIA SEADVVVHNG ALVHWVYPYE KLRSANVLST LATIDLASSG
KPKLLVFVSS TSAVDTEHYV QLSESLAQSS SEFTGVPEGD DLEGAKSSLK TGYGQTKWVS
EKLLFEAGRR GLRGHIVRPG YVVGDSRTAV TNTDDFIWRM VKGCVQLGLV PDINNTINMV
PVDHVALCTS LAAVSPLPNA PLSVLHITAS PLPTFNGMLS SLAHYGFLTE LCEYVVWRRK
LEQHVMEVQD NALFPLLHFV LDDLPTSTKA PELDDRNTRA ILKAHTGPTA KTVDEGLMGL
YLAWLVEAGF LPKPTLEKPE KRLPVLENAG NIKAAGRSGV
//
