ID A0A087XTE6_POEFO Unreviewed; 424 AA.
AC A0A087XTE6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-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};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000009049.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000009049.1}
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 EMBL; AYCK01005321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01005322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XTE6; -.
DR STRING; 48698.ENSPFOP00000009049; -.
DR Ensembl; ENSPFOT00000009061.1; ENSPFOP00000009049.1; ENSPFOG00000009068.1.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR OMA; DAAYNFN; -.
DR Proteomes; UP000028760; 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:SF0; 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:UP000028760}.
FT DOMAIN 137..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 369..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46552 MW; 36B6C89C68DAC415 CRC64;
HHLSSLHGVF FSCFASKSTL QTMCSRVWFV TDRRISQEYP QVQILRALKE RCADEDVEFR
YLLMDQIVLT ISQGQLGLRV EQELVTSYPQ VVLVRVPTPW VQSDSDITVL RHLEKMGCRL
INRPQAILNC VNKFWTFQEL AGHGVPLPDT YSYAGGHDNF RKMIDEAEPL GYPVVVKNAR
GHRGKAVFLA RDKHHLTDLC HLIRHDTPYL FQEYVKESHG RDVRVVLVGG RVVGSMLRCS
TDGRMQSNCS LGGVGMMCPL SEQGKQLAIE VSNILGMDVC GVDLLQLNDG SFVVCEANAN
VGFIAFDQAC GIDVAGIIAD FALSTLPSRL TRKMSLLSVV SSTSETSSEP EVCMVNAGGG
SLPEAVCNMS VGSSSSESDP ELAEPSQSSP RRSPASALSD LPDLPDAAYN FNNLLANEIK
LLTE
//