LYSY_DEIRA
ID LYSY_DEIRA Reviewed; 348 AA.
AC Q9RVQ9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=[LysW]-L-2-aminoadipate 6-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02083};
DE EC=1.2.1.103 {ECO:0000255|HAMAP-Rule:MF_02083};
GN Name=lysY {ECO:0000255|HAMAP-Rule:MF_02083}; OrderedLocusNames=DR_0963;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of [LysW]-
CC aminoadipate 6-phosphate to yield [LysW]-aminoadipate 6-semialdehyde.
CC {ECO:0000255|HAMAP-Rule:MF_02083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-N-(1-carboxy-5-
CC oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group
CC carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-
CC yl)-L-glutamine + H(+) + NADPH; Xref=Rhea:RHEA:41948, Rhea:RHEA-
CC COMP:9712, Rhea:RHEA-COMP:9714, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78499,
CC ChEBI:CHEBI:78501; EC=1.2.1.103; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02083};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5.
CC {ECO:0000255|HAMAP-Rule:MF_02083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02083}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. LysY sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_02083}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF10536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF10536.1; ALT_INIT; Genomic_DNA.
DR PIR; B75455; B75455.
DR RefSeq; NP_294687.2; NC_001263.1.
DR RefSeq; WP_010887608.1; NC_001263.1.
DR AlphaFoldDB; Q9RVQ9; -.
DR SMR; Q9RVQ9; -.
DR STRING; 243230.DR_0963; -.
DR EnsemblBacteria; AAF10536; AAF10536; DR_0963.
DR KEGG; dra:DR_0963; -.
DR PATRIC; fig|243230.17.peg.1150; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_0; -.
DR InParanoid; Q9RVQ9; -.
DR OMA; FSWRNNN; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00033; UER00037.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043870; F:N-acetyl-gamma-aminoadipyl-phosphate reductase activity; IEA:RHEA.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR HAMAP; MF_02083; LysY; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR037535; LysY.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01850; argC; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lysine biosynthesis; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..348
FT /note="[LysW]-L-2-aminoadipate 6-phosphate reductase"
FT /id="PRO_0000112500"
FT ACT_SITE 151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT BINDING 14..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT BINDING 315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
SQ SEQUENCE 348 AA; 37775 MW; 840EAEE18B423846 CRC64;
MSTEKKTVAI VGGSGYAGGE FLRLALGHPH LEVTQVTSER SAKLPVSMVH PNLRGATNLK
FRKAAELEEA DIIVLALPHN SAAKRITEFE AKGKVIVDLS ADFRLKDPEV YERFYGEPHP
APEQLGQWVY GNPELHREDL RGATRIACAG CFATSVILAL YPLLRLGALA PKDIIATGLV
GSSAAGASAS ESSHHPERAG SLRVYKPVGH RHTAEAQQEL PGKFPLHLTA ISTPRVRGIL
TTIQAWVPDG WSDKDVWSAY REVYGQEPFI RIVKVAKGIH RYPDPMLLDG TNFCDIGFEM
DVDTGRVVLM SAIDNLVKGT AGHAIQSLNV AQGWDERAGL GFLGLHPT
