ID I3R0M9_HALMT Unreviewed; 347 AA.
AC I3R0M9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase {ECO:0000256|HAMAP-Rule:MF_02083};
DE EC=1.2.1.103 {ECO:0000256|HAMAP-Rule:MF_02083};
DE EC=1.2.1.106 {ECO:0000256|HAMAP-Rule:MF_02083};
GN Name=argC {ECO:0000313|EMBL:AFK17789.1};
GN Synonyms=lysY {ECO:0000256|HAMAP-Rule:MF_02083};
GN OrderedLocusNames=HFX_0045 {ECO:0000313|EMBL:AFK17789.1};
GN ORFNames=BM92_09060 {ECO:0000313|EMBL:AHZ22783.1}, C439_10165
GN {ECO:0000313|EMBL:EMA02940.1}, E6P09_03320
GN {ECO:0000313|EMBL:QCQ74352.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK17789.1, ECO:0000313|Proteomes:UP000006469};
RN [1] {ECO:0000313|EMBL:AFK17789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK17789.1};
RX PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT "Identification of the haloarchaeal phasin (PhaP) that functions in
RT polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT mediterranei.";
RL Appl. Environ. Microbiol. 78:1946-1952(2012).
RN [2] {ECO:0000313|EMBL:AFK17789.1, ECO:0000313|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC {ECO:0000313|EMBL:AFK17789.1};
RX PubMed=22843593; DOI=10.1128/JB.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3] {ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000011603};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EMA02940.1, ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA02940.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000011603};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [5] {ECO:0000313|EMBL:AHZ22783.1, ECO:0000313|Proteomes:UP000027075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ22783.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000027075};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AFK17789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087;
RA Wang L., Yang H., Xiang H.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QCQ74352.1, ECO:0000313|Proteomes:UP000299011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ74352.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000299011};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_02083};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_02083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02083}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. LysY sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_02083}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02083}.
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DR EMBL; CP001868; AFK17789.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ22783.1; -; Genomic_DNA.
DR EMBL; AOLO01000007; EMA02940.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ74352.1; -; Genomic_DNA.
DR RefSeq; WP_004058744.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R0M9; -.
DR STRING; 523841.HFX_0045; -.
DR PaxDb; 523841-HFX_0045; -.
DR GeneID; 40155415; -.
DR KEGG; hme:HFX_0045; -.
DR PATRIC; fig|523841.21.peg.2063; -.
DR eggNOG; arCOG00495; Archaea.
DR HOGENOM; CLU_006384_0_1_2; -.
DR OrthoDB; 372053at2157; -.
DR UniPathway; UPA00033; UER00037.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0070401; F:NADP+ 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR32338:SF11; [LYSW]-L-2-AMINOADIPATE_[LYSW]-L-GLUTAMATE PHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_02083}; Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02083};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02083};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02083};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02083};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02083}.
FT DOMAIN 6..140
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 148
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
FT BINDING 311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02083"
SQ SEQUENCE 347 AA; 36984 MW; DAD29194624D907D CRC64;
MSEQLTAGVV GGSGFTGGEL LRLLDGHPNF EVAQATSRSY ERKTVGHVHP NLRHLDLRFT
SPADLESVDV LFTATPHGVS MEHIDAFQDA ADTVVDLSAD FRLSEETQYD EWYDGHICPE
YLEKSEYALP ELNRENLPGA DLIAAGGCNA TATILGLKPL FDADILSGDE QVVVDVKVGS
SEGGAGASKA SSHAERSGIV RPYAPTGHRH EAEIEEYLGL SVSFTVHAVD MVRGAAATCH
VFPDGPVSKG DMWKAFRGSY GDEPFMRTVA GGGGVYRYPE PKSVAGTNFG EVGFEIDPTN
RRLVVFSAID NMMKGSAGQA VHAANIALGL EETAGLDFTG YHPIGSP
//
