ID F4SAK2_MELLP Unreviewed; 1438 AA.
AC F4SAK2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=MELLADRAFT_54227 {ECO:0000313|EMBL:EGF98341.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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}.
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DR EMBL; GL883178; EGF98341.1; -; Genomic_DNA.
DR RefSeq; XP_007418372.1; XM_007418310.1.
DR STRING; 747676.F4SAK2; -.
DR EnsemblFungi; EGF98341; EGF98341; MELLADRAFT_54227.
DR GeneID; 18928902; -.
DR KEGG; mlr:MELLADRAFT_54227; -.
DR VEuPathDB; FungiDB:MELLADRAFT_54227; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_19_0_1; -.
DR InParanoid; F4SAK2; -.
DR OrthoDB; 3305653at2759; -.
DR UniPathway; UPA00033; UER00032.
DR Proteomes; UP000001072; 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 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; IPR013120; Far_NAD-bd.
DR InterPro; IPR014397; Lys2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; 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; 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:UP000001072}.
FT DOMAIN 902..982
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1438 AA; 159576 MW; 557A7B669CB8D857 CRC64;
MSDHTLARIA RRLSSLPSIA LPTDYPRPSH SASKKVVEAS IDVNLNHRAS LALARLSLHE
DGSPDPNSSS ERPNPPSPFH ILLATFLALL HRYTGETDIV VATSSRSADH PDPLLLRAEL
PPERSFWGLV RGIEQLEKEA EADHVPFETL LQTVGQREND TRDSPYTPLF RVRFLDAMDQ
TESHFINSTS MTTDLTIIVK SSVPSTPLVS SHEPMFPRPI SLTFLYNSLL FTSTRIHLMI
DQLSQLLIQA SMRPSAKLST IPFLTPSQLS LLPDPRQDLN WTTWPGPITR IFSANAQRHP
EKLCVSEHLI SQTAGDLSQP PQNRLRTFNY RQIDQASNIL AHQLLAGGIE PEDVVTIYST
RGVDLVVAIV GILKAGATFS VIDPAYPNQR QKIYLQVSRP RGLIVLERAG KLSQEVQAYI
DEELDIKLTI PALALQDDGH LLGGVSASGE DLLAPVQSTS DSAPDVSLGP DSVGTLSFTS
GSTGIPKGVK GRHFSLTHFF PWMATEFKLD SNSKFTMLSG IAHDPIQRDI FTPLFLGAEL
HIPTAEDIGT PGRLAEWMDD TQITVTHLTP AMGQLLSAQA TRIIPSLSNA FFVGDILTKR
DCTRLQQLAP NVQIINMFGT TETQRAVSYC PIPPISQDSI YLDTKKDIIP AGRGMKDVQL
LVVNRFEKNL QCGVGELGEI YVRSSGLAEG YLGPAEVSAE KFMPNWFTSN GAIGTDAKSN
QIEGKWLGVR DRVYKTGDLG RYLPDGTVEC VGRLDDQIKI RGFRIELGEI DTHLSQHPAI
RENVTLVRRD KDEEKILVSY FVPMKGQENE LISGSEVEEE EEEDVSELEK GIRKYRKLIK
DIREYLKTKL PTYSIPTLFV PLVRMPLNPN GKIDKPALPF PDTAKYLTAS QVKNSKKSTS
TTELTQTQST IQSIWQTLLP NNLYSNSIIP IDESFFDLGG HSILATRLVF EIRKMMAINA
PLGLVFENPT IGALAHQLDL LKNTDFGLAK DDEEKTGEES KATSDVATFD YAADSRMLMK
TLKPRYSKPQ WTDETPKTVL LTGVTGFLGA FILRELLSCP NQIGKVICHL RAKSKEAGLV
RLRESCESRG FWDESWMANG RVEIVLGDLE SRQIGLNDDL WKELSERVDL VVHNGALVHW
VYPYSKLRSA NVMATLSLIE FMAIGKSKAM TFVSSTAVLE KSHYVDLSDV LVQRGGRGIP
ETDDLEASAT GLTTGYGQTK WVSERLVMEA GRRGLCGSII RPAYIVGDSN TGVTNTDDFL
WRLVKGCVQI GAIPDIHNTV NMLPVNEVAR LTMLASTRNP NDLKVFHLTA RPLPRMNEFL
ETLKVYGYNV IKEDYLTWRI KLEQSVMDSG PEDNALFPLL HFVLNDLPTS TKSAELDDSN
TVQLIKNDDG DENRMTVNAE RIGIYLAWLV RVGFLPKPNG DDAFTLSKAN EREGVSTH
//
