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LYSY_THERP
ID   LYSY_THERP              Reviewed;         352 AA.
AC   B9KZP8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Putative [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}; Synonyms=argC;
GN   OrderedLocusNames=trd_1518;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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}.
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DR   EMBL; CP001275; ACM05243.1; -; Genomic_DNA.
DR   RefSeq; WP_015922465.1; NC_011959.1.
DR   AlphaFoldDB; B9KZP8; -.
DR   SMR; B9KZP8; -.
DR   STRING; 309801.trd_1518; -.
DR   EnsemblBacteria; ACM05243; ACM05243; trd_1518.
DR   KEGG; tro:trd_1518; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_0; -.
DR   OMA; FSWRNNN; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00033; UER00037.
DR   Proteomes; UP000000447; Chromosome.
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:0046983; F:protein dimerization activity; 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   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 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.
FT   CHAIN           1..352
FT                   /note="Putative [LysW]-L-2-aminoadipate 6-phosphate
FT                   reductase"
FT                   /id="PRO_1000123253"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT   BINDING         11..14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT   BINDING         319
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
SQ   SEQUENCE   352 AA;  38377 MW;  A3FE5E9B5EFC8833 CRC64;
     MVVSVAILGG SGYTGGELLR LLLSHPEVEV KQVTSRSRAG KFVHTVHPNL RKRTALKFVP
     PEALEPVDLL FACLPHGETA PIVDRLLELA PIVIDLSADF RLRDPAAYEQ WYHWTHPRPD
     LLAQAVYGLP ELHREEIRNA RYIACPGCNS TTVILGLAPL FRAGLIDLDL PVTVECKVGS
     SGAGGEAGPA SHHPERSGVI RPFKPGGHRH TAEVLQELTV CGRTPSLGLS VTSVEAVRGI
     LATAHLFPKQ PLTDRDLWQV YRAAYGQEPF IRLVKEASGI HRYPEPKILA GSNYCDIGWE
     LDELPGGRQR LVVMSAIDNL MKGAAGQAVQ AMNIRLGFPE TLGLEFPGLH PL
 
 
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