NAGS_DANRE
ID NAGS_DANRE Reviewed; 527 AA.
AC E7FCP8;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=N-acetylglutamate synthase, mitochondrial {ECO:0000305};
DE EC=2.3.1.1 {ECO:0000269|PubMed:24465614};
DE Contains:
DE RecName: Full=N-acetylglutamate synthase, mature form {ECO:0000303|PubMed:24465614};
DE Short=NAGS-M {ECO:0000303|PubMed:24465614};
DE Contains:
DE RecName: Full=N-acetylglutamate synthase, conserved domain form {ECO:0000303|PubMed:24465614};
DE Short=NAGS-C {ECO:0000303|PubMed:24465614};
DE Flags: Precursor;
GN Name=nags {ECO:0000312|ZFIN:ZDB-GENE-121219-2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=24465614; DOI=10.1371/journal.pone.0085597;
RA Caldovic L., Haskins N., Mumo A., Majumdar H., Pinter M., Tuchman M.,
RA Krufka A.;
RT "Expression pattern and biochemical properties of zebrafish N-
RT acetylglutamate synthase.";
RL PLoS ONE 9:E85597-E85597(2014).
CC -!- FUNCTION: Plays a role in the regulation of ureagenesis by producing
CC the essential cofactor N-acetylglutamate (NAG), thus modulating
CC carbamoylphosphate synthase I (cps1) activity.
CC {ECO:0000305|PubMed:24465614}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000269|PubMed:24465614};
CC -!- ACTIVITY REGULATION: Inhibited by L-arginine.
CC {ECO:0000269|PubMed:24465614}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for acetyl-CoA {ECO:0000269|PubMed:24465614};
CC KM=1.13 mM for L-glutamate {ECO:0000269|PubMed:24465614};
CC -!- SUBUNIT: Homodimer (By similarity). Homotetramer (PubMed:24465614).
CC {ECO:0000250|UniProtKB:Q8N159, ECO:0000269|PubMed:24465614}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q8N159}.
CC -!- DEVELOPMENTAL STAGE: Detected in 32-cell embryos, probably due to
CC perdurance of maternal transcripts. Has low expression at the 90%
CC epiboly and tailbud stages (9-10 hours post-fertilization, hpf).
CC Moderately expressed from 24 hpf onwards, and strongly expressed at the
CC adult stage. {ECO:0000269|PubMed:24465614}.
CC -!- DOMAIN: The amino-acid kinase (AAK) domain mediates binding of L-
CC arginine. {ECO:0000250|UniProtKB:Q8N159}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AL935200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_685919.3; XM_680827.8.
DR AlphaFoldDB; E7FCP8; -.
DR SMR; E7FCP8; -.
DR STRING; 7955.ENSDARP00000101563; -.
DR PaxDb; E7FCP8; -.
DR Ensembl; ENSDART00000110343; ENSDARP00000101563; ENSDARG00000077193.
DR GeneID; 557716; -.
DR KEGG; dre:557716; -.
DR CTD; 162417; -.
DR ZFIN; ZDB-GENE-121219-2; nags.
DR eggNOG; KOG2436; Eukaryota.
DR GeneTree; ENSGT00390000005602; -.
DR HOGENOM; CLU_034853_0_0_1; -.
DR InParanoid; E7FCP8; -.
DR OMA; FQTCYHS; -.
DR OrthoDB; 769117at2759; -.
DR PhylomeDB; E7FCP8; -.
DR TreeFam; TF332628; -.
DR Reactome; R-DRE-70635; Urea cycle.
DR PRO; PR:E7FCP8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000077193; Expressed in ovary and 8 other tissues.
DR ExpressionAtlas; E7FCP8; baseline.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IDA:ZFIN.
DR GO; GO:0034618; F:arginine binding; IDA:ZFIN.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006536; P:glutamate metabolic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011243; GlcNAc_Synth_met.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR Pfam; PF04768; NAT; 1.
DR PIRSF; PIRSF036442; NAGS_animal; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide; Urea cycle.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..527
FT /note="N-acetylglutamate synthase, mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444987"
FT CHAIN 84..527
FT /note="N-acetylglutamate synthase, conserved domain form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444988"
FT DOMAIN 360..511
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 28..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..361
FT /note="Amino-acid kinase domain (AAK)"
FT /evidence="ECO:0000250|UniProtKB:Q8N159"
FT REGION 40..83
FT /note="May stabilize the oligomeric structure"
FT /evidence="ECO:0000269|PubMed:24465614"
FT COMPBIAS 44..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR036442-1"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR036442-1"
FT BINDING 459..464
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N159"
SQ SEQUENCE 527 AA; 58407 MW; 657FE482B70566D3 CRC64;
MAKVNSGSSG CRAMVMAGQF WTKPFALSSQ RSGPHRRSAA EVNRRMSSSR TAGHGSKTPL
WSQQESYNHS SLGERSAWSN RTLIYRDVKA FLREIGGDPR EARYWLTHFQ RAGSTPAFAV
LEVDPSVFDS HEMVQSLAFG LSFLQRMDMK LVVVMGLPAE ITEDDHTRSA TDSPLARTVM
VKHCQALTEA LQDNSANVMP FFSSEALLQL QDNPLDGSSS GPSVVVDSAL LQWTLDCRVI
PLVCPVGRDT TGRSSVLRSI QVTTAISQTL QPLKVIFLNS SGGIRNQNHK VLGLVSLPGD
LPALSCAEWL NEVEQKRIGS IAELLNLLPV ESSAVLTSAN TLLTELFSHK GSGTLFKNGD
PIRRYSSLED IDVDRLLALI NKSFEKNLRE DYIASLEGRL HSVYLSEGYS AAAIITTEPV
NSGTPYLDKF VVSSSKQGQG TGQILWECIR QDFSKLFWRS RTTNRINPWY FKHCDGSFVN
GHWIVFWLGL SDIRESYELV EFAKSHPDSF CSLSTTETKP LQQHHGS
