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[LysW]-L-2-aminoadipate 6-phosphate reductase (EC 1.2.1.-)

 LYSY_THET2              Reviewed;         344 AA.
O50146; Q9ZND6;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 126.
RecName: Full=[LysW]-L-2-aminoadipate 6-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000305};
EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:26966182, ECO:0000305|PubMed:19620981};
Name=lysY {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000303|PubMed:19620981};
Synonyms=argC {ECO:0000303|PubMed:10074061,
ECO:0000303|PubMed:9418242}; OrderedLocusNames=TT_C1542;
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
Thermus.
NCBI_TaxID=262724;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
PubMed=15064768; DOI=10.1038/nbt956;
Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
"The genome sequence of the extreme thermophile Thermus
thermophilus.";
Nat. Biotechnol. 22:547-553(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236.
PubMed=10074061;
Kobashi N., Nishiyama M., Tanokura M.;
"Aspartate kinase-independent lysine synthesis in an extremely
thermophilic bacterium, Thermus thermophilus: lysine is synthesized
via alpha-aminoadipic acid not via diaminopimelic acid.";
J. Bacteriol. 181:1713-1718(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-344.
STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
PubMed=9418242; DOI=10.1111/j.1574-6968.1997.tb12755.x;
Kosuge T., Hoshino T.;
"Molecular cloning and sequence analysis of the lysR gene from the
extremely thermophilic eubacterium, Thermus thermophilus HB27.";
FEMS Microbiol. Lett. 157:73-79(1997).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
PubMed=19620981; DOI=10.1038/nchembio.198;
Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R.,
Fujimura T., Nishiyama C., Kuzuyama T., Nishiyama M.;
"Discovery of proteinaceous N-modification in lysine biosynthesis of
Thermus thermophilus.";
Nat. Chem. Biol. 5:673-679(2009).
[5] {ECO:0000244|PDB:5EIN, ECO:0000244|PDB:5EIO}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH LYSW-AASA AND
NADP AND OF MUTANT ALA-148 IN COMPLEX WITH SUBSTRATE ANALOG AND NADP,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
INTERACTION WITH LYSW, AND MUTAGENESIS OF ARG-102; CYS-148; ARG-195;
HIS-209; ARG-258; LYS-271 AND ARG-278.
STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
PubMed=26966182; DOI=10.1074/jbc.M115.707034;
Shimizu T., Tomita T., Kuzuyama T., Nishiyama M.;
"Crystal structure of the LysYLysW complex from Thermus
thermophilus.";
J. Biol. Chem. 291:9948-9959(2016).
-!- FUNCTION: Catalyzes the NADPH-dependent reduction of [LysW]-
aminoadipate 6-phosphate to yield [LysW]-aminoadipate 6-
semialdehyde. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000269|PubMed:26966182, ECO:0000305|PubMed:19620981}.
-!- CATALYTIC ACTIVITY: [LysW]-C-terminal-L-glutamyl-gamma-L-2-
aminoadipate 6-phosphate + H(+) + NADPH = [LysW]-C-terminal-L-
glutamyl-gamma-L-2-aminoadipate 6-semialdehyde + NADP(+) +
phosphate. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000269|PubMed:26966182, ECO:0000305|PubMed:19620981}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.8 uM for [LysW]-aminoadipate 6-semialdehyde
{ECO:0000269|PubMed:26966182};
KM=14 uM for NADP(+) {ECO:0000269|PubMed:26966182};
KM=12000 uM for phosphate {ECO:0000269|PubMed:26966182};
Note=kcat is 0.96 sec(-1). {ECO:0000269|PubMed:26966182};
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step
3/5. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000269|PubMed:19620981}.
-!- SUBUNIT: Homotetramer (PubMed:26966182). Interacts with LysW. May
form a ternary complex with LysW and LysZ (PubMed:26966182).
{ECO:0000269|PubMed:26966182}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02083}.
-!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
subfamily. LysY sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA23878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AE017221; AAS81884.1; -; Genomic_DNA.
EMBL; AB017109; BAA74767.1; -; mRNA.
EMBL; AB006681; BAA23878.1; ALT_INIT; Genomic_DNA.
PIR; T43947; T43947.
RefSeq; WP_011173916.1; NC_005835.1.
PDB; 5EIN; X-ray; 1.70 A; A/B=1-344.
PDB; 5EIO; X-ray; 1.80 A; A/B=1-344.
PDBsum; 5EIN; -.
PDBsum; 5EIO; -.
ProteinModelPortal; O50146; -.
SMR; O50146; -.
STRING; 262724.TTC1542; -.
EnsemblBacteria; AAS81884; AAS81884; TT_C1542.
KEGG; tth:TT_C1542; -.
eggNOG; ENOG4105C0N; Bacteria.
eggNOG; COG0002; LUCA.
KO; K05829; -.
OMA; FSWRNNN; -.
BioCyc; MetaCyc:MONOMER-6802; -.
UniPathway; UPA00033; UER00037.
Proteomes; UP000000592; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
HAMAP; MF_00150; ArgC_type1; 1.
HAMAP; MF_02083; LysY; 1.
InterPro; IPR023013; AGPR_AS.
InterPro; IPR000706; AGPR_type-1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
Pfam; PF01118; Semialdhyde_dh; 1.
Pfam; PF02774; Semialdhyde_dhC; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01850; argC; 1.
PROSITE; PS01224; ARGC; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm;
Lysine biosynthesis; NADP; Oxidoreductase.
CHAIN 1 344 [LysW]-L-2-aminoadipate 6-phosphate
reductase.
/FTId=PRO_0000112501.
NP_BIND 12 15 NADP. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000269|PubMed:26966182}.
NP_BIND 36 38 NADP. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000269|PubMed:26966182}.
ACT_SITE 148 148 {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000305|PubMed:26966182}.
BINDING 75 75 NADP; via carbonyl oxygen.
{ECO:0000269|PubMed:26966182}.
BINDING 180 180 NADP; via carbonyl oxygen.
{ECO:0000269|PubMed:26966182}.
BINDING 184 184 NADP; via amide nitrogen.
{ECO:0000269|PubMed:26966182}.
BINDING 312 312 NADP. {ECO:0000255|HAMAP-Rule:MF_02083,
ECO:0000269|PubMed:26966182}.
MUTAGEN 102 102 R->A: Strong decrease in activity.
{ECO:0000269|PubMed:26966182}.
MUTAGEN 148 148 C->A: Lack of activity.
{ECO:0000269|PubMed:26966182}.
MUTAGEN 195 195 R->A: 5-fold decrease in kcat and 40-fold
increase in Km for [LysW]-aminoadipate 6-
semialdehyde.
{ECO:0000269|PubMed:26966182}.
MUTAGEN 209 209 H->A: Does not affect activity under
basic conditions. Strong decrease of
activity under neutral conditions.
{ECO:0000269|PubMed:26966182}.
MUTAGEN 258 258 R->A: Slight decrease in kcat and 17-fold
increase in Km for [LysW]-aminoadipate 6-
semialdehyde.
{ECO:0000269|PubMed:26966182}.
MUTAGEN 271 271 K->A: 5-fold decrease in kcat and 70-fold
increase in Km for [LysW]-aminoadipate 6-
semialdehyde.
{ECO:0000269|PubMed:26966182}.
MUTAGEN 278 278 R->A: Lack of activity.
{ECO:0000269|PubMed:26966182}.
STRAND 4 10 {ECO:0000244|PDB:5EIN}.
HELIX 14 24 {ECO:0000244|PDB:5EIN}.
STRAND 29 35 {ECO:0000244|PDB:5EIN}.
TURN 38 41 {ECO:0000244|PDB:5EIN}.
HELIX 44 46 {ECO:0000244|PDB:5EIN}.
HELIX 49 51 {ECO:0000244|PDB:5EIN}.
TURN 52 54 {ECO:0000244|PDB:5EIN}.
HELIX 62 64 {ECO:0000244|PDB:5EIN}.
STRAND 69 73 {ECO:0000244|PDB:5EIN}.
HELIX 79 82 {ECO:0000244|PDB:5EIN}.
HELIX 84 88 {ECO:0000244|PDB:5EIN}.
STRAND 92 96 {ECO:0000244|PDB:5EIN}.
TURN 100 102 {ECO:0000244|PDB:5EIN}.
HELIX 106 113 {ECO:0000244|PDB:5EIN}.
HELIX 119 121 {ECO:0000244|PDB:5EIN}.
STRAND 124 127 {ECO:0000244|PDB:5EIO}.
HELIX 130 137 {ECO:0000244|PDB:5EIN}.
STRAND 141 144 {ECO:0000244|PDB:5EIN}.
HELIX 148 163 {ECO:0000244|PDB:5EIN}.
STRAND 171 177 {ECO:0000244|PDB:5EIN}.
HELIX 179 182 {ECO:0000244|PDB:5EIN}.
HELIX 188 190 {ECO:0000244|PDB:5EIN}.
HELIX 192 195 {ECO:0000244|PDB:5EIN}.
STRAND 200 205 {ECO:0000244|PDB:5EIN}.
HELIX 210 215 {ECO:0000244|PDB:5EIN}.
STRAND 223 229 {ECO:0000244|PDB:5EIN}.
STRAND 236 244 {ECO:0000244|PDB:5EIN}.
HELIX 250 261 {ECO:0000244|PDB:5EIN}.
STRAND 267 269 {ECO:0000244|PDB:5EIN}.
STRAND 273 276 {ECO:0000244|PDB:5EIN}.
HELIX 282 285 {ECO:0000244|PDB:5EIN}.
STRAND 291 297 {ECO:0000244|PDB:5EIN}.
TURN 299 301 {ECO:0000244|PDB:5EIN}.
STRAND 303 310 {ECO:0000244|PDB:5EIN}.
TURN 312 317 {ECO:0000244|PDB:5EIN}.
HELIX 318 329 {ECO:0000244|PDB:5EIN}.
TURN 333 336 {ECO:0000244|PDB:5EIN}.
SEQUENCE 344 AA; 38051 MW; B11CE66CB2F04C15 CRC64;
MDKKTLSIVG ASGYAGGEFL RLALSHPYLE VKQVTSRRFA GEPVHFVHPN LRGRTNLKFI
PPEKLEPADI LVLALPHGVF AREFDRYSAL APILIDLSAD FRLKDPELYR RYYGEHPRPD
LLGCFVYAVP ELYREALKGA DWIAGAGCNA TATLLGLYPL LKAGVLKPTP IFVTLLISTS
AAGAEASPAS HHPERAGSIR VYKPTGHRHT AEVVENLPGR PEVHLTAIAT DRVRGILMTA
QCFVQDGWSE RDVWQAYREA YAGEPFIRLV KQKKGVHRYP DPRFVQGTNY ADIGFELEED
TGRLVVMTAI DNLVKGTAGH ALQALNVRMG WPETLGLDFP GLHP


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