ID   G1KTW5_ANOCA            Unreviewed;       386 AA.
AC   G1KTW5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=N-acetylaspartylglutamate synthase {ECO:0000256|ARBA:ARBA00012938};
DE            EC=6.3.2.41 {ECO:0000256|ARBA:ARBA00012938};
GN   Name=RIMKLB {ECO:0000313|Ensembl:ENSACAP00000017160.4};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000017160.4, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000017160.4, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000017160.4,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000017160.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-
CC         acetyl-L-aspartyl-L-glutamate + phosphate; Xref=Rhea:RHEA:40035,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931,
CC         ChEBI:CHEBI:456216; EC=6.3.2.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00000622};
CC   -!- SIMILARITY: Belongs to the RimK family.
CC       {ECO:0000256|ARBA:ARBA00007854}.
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DR   RefSeq; XP_016846649.1; XM_016991160.1.
DR   AlphaFoldDB; G1KTW5; -.
DR   STRING; 28377.ENSACAP00000017160; -.
DR   Ensembl; ENSACAT00000017497.4; ENSACAP00000017160.4; ENSACAG00000017434.4.
DR   GeneID; 100563778; -.
DR   KEGG; acs:100563778; -.
DR   CTD; 57494; -.
DR   eggNOG; ENOG502QT4M; Eukaryota.
DR   GeneTree; ENSGT00390000014577; -.
DR   HOGENOM; CLU_054353_3_1_1; -.
DR   InParanoid; G1KTW5; -.
DR   TreeFam; TF332035; -.
DR   Proteomes; UP000001646; Chromosome 2.
DR   Bgee; ENSACAG00000017434; Expressed in testis and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0072591; F:citrate-L-glutamate ligase activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0072590; F:N-acetyl-L-aspartate-L-glutamate ligase activity; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR   NCBIfam; TIGR00768; rimK_fam; 1.
DR   PANTHER; PTHR21621:SF5; BETA-CITRYLGLUTAMATE SYNTHASE B; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT   DOMAIN          119..304
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          325..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  42598 MW;  B17DA8DDCD3BD2E3 CRC64;
     MCSSIAPRIW FLTDRRIRED YPQQEILRAL KAKCCEEDLE FRALVIDEVV LTIEQGNLGL
     RVNGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
     ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
     SHLIRHEAPY LFQKYVQESH GKDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGIGMMCS
     LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFYVCEANA NVGFIAFDKA CNLDVAGIIA
     DYAASLLPPG RLTRRMSLLS VVSTASETSE PELGPPASAT VDNMSASSSS VDSDPETTER
     ELLTKLPGGI FNMNQLIANE IKLLVE
//