ID A0A1H6IWR4_9EURY Unreviewed; 309 AA.
AC A0A1H6IWR4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Putative [LysW]-aminoadipate/[LysW]-glutamate kinase {ECO:0000256|HAMAP-Rule:MF_02082};
DE EC=2.7.2.17 {ECO:0000256|HAMAP-Rule:MF_02082};
DE EC=2.7.2.19 {ECO:0000256|HAMAP-Rule:MF_02082};
GN Name=lysZ {ECO:0000256|HAMAP-Rule:MF_02082};
GN ORFNames=SAMN05192561_103291 {ECO:0000313|EMBL:SEH50896.1};
OS Halopenitus malekzadehii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1267564 {ECO:0000313|EMBL:SEH50896.1, ECO:0000313|Proteomes:UP000199215};
RN [1] {ECO:0000313|EMBL:SEH50896.1, ECO:0000313|Proteomes:UP000199215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10418 {ECO:0000313|EMBL:SEH50896.1,
RC ECO:0000313|Proteomes:UP000199215};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. Phosphorylates the LysW-bound precursors glutamate (for
CC arginine biosynthesis), respectively alpha-aminoadipate (for lysine
CC biosynthesis). {ECO:0000256|HAMAP-Rule:MF_02082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-N-(1,4-
CC dicarboxybutan-1-yl)-L-glutamine + ATP = [amino-group carrier
CC protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-
CC glutamine + ADP; Xref=Rhea:RHEA:41944, Rhea:RHEA-COMP:9694,
CC Rhea:RHEA-COMP:9712, ChEBI:CHEBI:30616, ChEBI:CHEBI:78499,
CC ChEBI:CHEBI:78503, ChEBI:CHEBI:456216; EC=2.7.2.17;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-glutamyl)-L-
CC glutamate + ATP = [amino-group carrier protein]-C-terminal-gamma-(5-
CC phospho-L-glutamyl)-L-glutamate + ADP; Xref=Rhea:RHEA:52632,
CC Rhea:RHEA-COMP:13311, Rhea:RHEA-COMP:13313, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:136714, ChEBI:CHEBI:136717, ChEBI:CHEBI:456216;
CC EC=2.7.2.19; Evidence={ECO:0000256|HAMAP-Rule:MF_02082};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02082}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 2/5.
CC {ECO:0000256|HAMAP-Rule:MF_02082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02082}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. LysZ
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02082}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02082}.
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DR EMBL; FNWU01000003; SEH50896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6IWR4; -.
DR STRING; 1267564.SAMN05192561_103291; -.
DR OrthoDB; 6816at2157; -.
DR UniPathway; UPA00033; UER00036.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000199215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043744; F:N2-acetyl-L-aminoadipate kinase activity; IEA:RHEA.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR HAMAP; MF_02082; LysZ; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR037529; LysZ.
DR NCBIfam; TIGR00761; argB; 1.
DR PANTHER; PTHR23342:SF19; [LYSW]-AMINOADIPATE KINASE; 1.
DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_02082}; Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02082};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02082}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02082};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_02082};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02082}; Reference proteome {ECO:0000313|Proteomes:UP000199215};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02082}.
FT DOMAIN 11..261
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT REGION 284..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02082"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02082"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02082"
FT SITE 242
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02082"
SQ SEQUENCE 309 AA; 31026 MW; 70B0CC8085680162 CRC64;
MSAAESTDPP VVVKVGGAKA VDPAGAIGDV ARLVAEGREV VVVHGGSTAV DGMLDRLGID
PEYVESASGV TGRFTDAETM EVFEMVMAGK LNTELVASLQ EADVDAVGLS GVDGGLLSGP
RKSAVRVVED GKKKIRRGDH SGKPESVNAA LLEELTADGY VPVVSPPMAG QERDGGVTPV
NTDADRAAAA IAGALGAELV LLTDVSGVYA DPDDPTTLID SVSTPVDLEA LESAAEGFMG
KKVMAAEEAL STGSPRVVVA DANAADPIVD ALAGGGTHVH ASALADTNED DNDAQVDDGA
QEDATTGGA
//
