LYSY_NITMS
ID LYSY_NITMS Reviewed; 348 AA.
AC A9A1K6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02083};
DE EC=1.2.1.103 {ECO:0000255|HAMAP-Rule:MF_02083};
DE EC=1.2.1.106 {ECO:0000255|HAMAP-Rule:MF_02083};
GN Name=lysY {ECO:0000255|HAMAP-Rule:MF_02083}; OrderedLocusNames=Nmar_1289;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {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 -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-glutamyl-5-
CC semialdehyde)-L-glutamate + NADP(+) + phosphate = [amino-group
CC carrier protein]-C-terminal-gamma-(5-phospho-L-glutamyl)-L-glutamate
CC + H(+) + NADPH; Xref=Rhea:RHEA:52668, Rhea:RHEA-COMP:13313,
CC Rhea:RHEA-COMP:13327, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:136717,
CC ChEBI:CHEBI:136761; EC=1.2.1.106; 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
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; CP000866; ABX13185.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A1K6; -.
DR SMR; A9A1K6; -.
DR STRING; 436308.Nmar_1289; -.
DR EnsemblBacteria; ABX13185; ABX13185; Nmar_1289.
DR KEGG; nmr:Nmar_1289; -.
DR eggNOG; arCOG00495; Archaea.
DR HOGENOM; CLU_006384_0_1_2; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; A9A1K6; -.
DR UniPathway; UPA00033; UER00037.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000792; 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:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lysine biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..348
FT /note="Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate
FT phosphate reductase"
FT /id="PRO_1000096733"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02083"
FT BINDING 9..12
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; 38795 MW; FA9498B737304BB2 CRC64;
MKVGVVGASG YVGGETLRLL VNHPNVEITM VTSRQHVGEY LHRVQPSLKG FTDLTFSELD
YDKLTDKCDL VFTAVPHGTA TEIVKALYDR GIKIIDLSAD YRLHDQDAYD KWYGWEHPHP
DYLNKSVFGV PELHREEIKK AQLVSCPGCM AVTSMLALAP LIRNNIIDTD HIVVDSKIGS
SGAGSGSGTA HAMRAGVIRP YKPAKHRHTG EIEQELSEIA GKKIHVSMSP HAVDVVRGIL
CTNHTFMQKD MEEKELWKLY RQTYGEEKFV RLIRDKKGLY KFPDPKFLVG SNFCDIGFDL
DEDNNRLIAL SASDNLMKGA AGSAIQNMNV MCGFDEMDGL RYTPLTPV
