ID A0A2K6F0P7_PROCO Unreviewed; 386 AA.
AC A0A2K6F0P7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:ENSPCOP00000007534.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000007534.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000007534.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_012493376.1; XM_012637922.1.
DR AlphaFoldDB; A0A2K6F0P7; -.
DR STRING; 379532.ENSPCOP00000007534; -.
DR Ensembl; ENSPCOT00000018078.1; ENSPCOP00000007534.1; ENSPCOG00000015009.1.
DR GeneID; 105805100; -.
DR KEGG; pcoq:105805100; -.
DR CTD; 57494; -.
DR GeneTree; ENSGT00390000014577; -.
DR OrthoDB; 4026633at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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; IEA:Ensembl.
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:UP000233160}.
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; 42492 MW; D25B7D5B1308445D CRC64;
MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEVV LTIEQGNLGL
RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
SHLIRHEAPY LFQKYIKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS
LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA
DYAASLLPSG RLTRRMSLLS VVSTASETSE PELGPPASTA VDNMSASSSS VDSDPESTER
ELLTKLPGGL FNMNQLLANE IKLLVE
//
