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Database: UniProt
Entry: A0A093PPC1_9PASS
LinkDB: A0A093PPC1_9PASS
Original site: A0A093PPC1_9PASS 
ID   A0A093PPC1_9PASS        Unreviewed;       386 AA.
AC   A0A093PPC1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=N-acetylaspartylglutamate synthase {ECO:0000256|ARBA:ARBA00012938};
DE            EC=6.3.2.41 {ECO:0000256|ARBA:ARBA00012938};
GN   ORFNames=N305_14281 {ECO:0000313|EMBL:KFW78633.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78633.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW78633.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78633.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL670305; KFW78633.1; -; Genomic_DNA.
DR   RefSeq; XP_008919374.1; XM_008921126.2.
DR   RefSeq; XP_017941081.1; XM_018085592.1.
DR   AlphaFoldDB; A0A093PPC1; -.
DR   STRING; 328815.ENSMVIP00005020128; -.
DR   GeneID; 103755209; -.
DR   CTD; 57494; -.
DR   OrthoDB; 4026633at2759; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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:UP000053258}.
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;  42567 MW;  4AEB9A26DAC58543 CRC64;
     MCSSVAPRLW FLTDRRIRED YPQQEILRAL KAKCCEEELD FRALVMDEVV LTIEDGNLGL
     RVKGELVTSY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
     ELAGHGVPLP DTFSYGGHEN FSKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
     SHLIRHDAPY LFQKYVKESH GKDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS
     LSEQGKQLAV QVSNILGMDV CGIDLLMKDD GSFYVCEANA NVGFIAFDKA CNLDVAGIIA
     DYAASLLTPG RLTRRMSLLS VVSTASETSE PELGPPASAA VDNMSASSSS VDSDPETTER
     ELLTKLPGAL FNMNQLLANE IKLLVE
//
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