ID U3JXT2_FICAL Unreviewed; 386 AA.
AC U3JXT2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 39.
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:ENSFALP00000007586.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000007586.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000007586.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000007586.2}
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_005038323.1; XM_005038266.1.
DR RefSeq; XP_005038324.1; XM_005038267.1.
DR AlphaFoldDB; U3JXT2; -.
DR STRING; 59894.ENSFALP00000007586; -.
DR Ensembl; ENSFALT00000007618.2; ENSFALP00000007586.2; ENSFALG00000007270.2.
DR GeneID; 101814507; -.
DR KEGG; fab:101814507; -.
DR CTD; 57494; -.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_1_1; -.
DR Proteomes; UP000016665; Chromosome 1.
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:UP000016665}.
FT DOMAIN 119..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 325..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 42505 MW; 91A3BA49B196FBB6 CRC64;
MCSSVAPRLW FLTDRRIRED YPQQEILRAL KAKCCEEELD FRALVMDEVV LTIEDGNLGL
RVKGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
ELAGHGVPLP DTFSYGGHEN FSKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
SHLIRHDAPY LFQKYVKESH GKDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS
LSEQGKQLAV QVSNILGMDV CGIDLLMKDD GSFYVCEANA NVGFIAFDKA CNLDVAGIIA
DYAASLLAPG RLTRRMSLLS VVSTASETSE PELGPPAGAA VDNMSASSSS VDSDPETTER
ELLTKLPGAL FNMNQLLANE IKLLVE
//
