ID A0A498MJK4_LABRO Unreviewed; 176 AA.
AC A0A498MJK4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=N-acetylaspartate synthetase {ECO:0000256|ARBA:ARBA00041029};
DE EC=2.3.1.17 {ECO:0000256|ARBA:ARBA00039136};
DE AltName: Full=N-acetyltransferase 8-like protein {ECO:0000256|ARBA:ARBA00043248};
GN ORFNames=ROHU_024127 {ECO:0000313|EMBL:RXN21548.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN21548.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN21548.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN21548.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN21548.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00035927};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14166;
CC Evidence={ECO:0000256|ARBA:ARBA00035927};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004304}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000256|ARBA:ARBA00038470}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN21548.1}.
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DR EMBL; QBIY01012612; RXN21548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MJK4; -.
DR STRING; 84645.A0A498MJK4; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR13947; GNAT FAMILY N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR13947:SF11; N-ACETYLASPARTATE SYNTHETASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MJK4};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 20..163
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 176 AA; 20251 MW; 06EACF8C026967C3 CRC64;
MCYVMTKSFT LTFCTPFILM GARYYYSRKV ILNYLDCALH TDMADIEAYY MKPTGSCFWV
AVLQGQVVGI VAAQGREDDN TVELRRMSVD SRFRGKGIAK ALGRRVLEFA MLNNYSAVVL
GTTAVKMAAH KLYESLGFRR VGETEDYTLP GMTRSPLERL FFQIRYSRYR LQLHEE
//
