NAT8L_XENTR
ID NAT8L_XENTR Reviewed; 271 AA.
AC A4II32;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=N-acetylaspartate synthetase;
DE Short=NAA synthetase;
DE EC=2.3.1.17 {ECO:0000250|UniProtKB:Q8N9F0};
DE AltName: Full=N-acetyltransferase 8-like protein;
GN Name=nat8l;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of N-acetylaspartate acid (NAA) from
CC L-aspartate and acetyl-CoA. {ECO:0000250|UniProtKB:Q8N9F0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-aspartate = CoA + H(+) + N-acetyl-L-aspartate;
CC Xref=Rhea:RHEA:14165, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q8N9F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14166;
CC Evidence={ECO:0000250|UniProtKB:Q8N9F0};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F0}.
CC Microsome membrane {ECO:0000250|UniProtKB:D3ZVU9}; Single-pass membrane
CC protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q8N9F0}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q3UGX3}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the camello family. {ECO:0000305}.
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DR EMBL; BC135824; AAI35825.1; -; mRNA.
DR RefSeq; NP_001096350.1; NM_001102880.1.
DR AlphaFoldDB; A4II32; -.
DR SMR; A4II32; -.
DR STRING; 8364.ENSXETP00000052747; -.
DR PaxDb; A4II32; -.
DR DNASU; 100124940; -.
DR GeneID; 100124940; -.
DR KEGG; xtr:100124940; -.
DR CTD; 339983; -.
DR Xenbase; XB-GENE-5817008; nat8l.
DR eggNOG; KOG3139; Eukaryota.
DR InParanoid; A4II32; -.
DR OrthoDB; 1341682at2759; -.
DR Reactome; R-XTR-8963693; Aspartate and asparagine metabolism.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0017188; F:aspartate N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Endoplasmic reticulum; Membrane; Microsome;
KW Mitochondrion; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..271
FT /note="N-acetylaspartate synthetase"
FT /id="PRO_0000305232"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 115..258
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 271 AA; 30726 MW; 071F172B3192BC95 CRC64;
MTYRGTRKSP CCSPPPRCGP PLPSGPAGSA LGPPSSGAEE EMTKEQVYLR EFQPADQEFA
RRIFYEGIKE RILSSAFRGL KYQPLLQSVY AVIIIMCFVV TKSLLVTCCM PLFLLGMRYY
YSRKIILNHL ECALRTDMSD IEQYYMKQPG SCFWVAVLEG KVVGIVAARG NEEDNVVELR
RMSVDSNYRG KGIAKALGRK VLEFAMLNHY SSIVLGTTAV KIAAHKLYES LGFKHVGVVE
HHIVPGMTHS LLERLFFQLR YHRYCLQLRE E