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Database: UniProt
Entry: G8JTN3_ERECY
LinkDB: G8JTN3_ERECY
Original site: G8JTN3_ERECY 
ID   G8JTN3_ERECY            Unreviewed;       859 AA.
AC   G8JTN3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51731};
GN   OrderedLocusNames=Ecym_4323 {ECO:0000313|EMBL:AET39386.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS   NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET39386.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000256|ARBA:ARBA00004828,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000256|ARBA:ARBA00004862,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007239,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC       kinase family. {ECO:0000256|ARBA:ARBA00006830,
CC       ECO:0000256|PIRNR:PIRNR036440}.
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DR   EMBL; CP002500; AET39386.1; -; Genomic_DNA.
DR   RefSeq; XP_003646203.1; XM_003646155.1.
DR   AlphaFoldDB; G8JTN3; -.
DR   STRING; 931890.G8JTN3; -.
DR   GeneID; 11469500; -.
DR   KEGG; erc:Ecym_4323; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   eggNOG; KOG4354; Eukaryota.
DR   HOGENOM; CLU_006384_4_0_1; -.
DR   InParanoid; G8JTN3; -.
DR   OMA; IAFIPHV; -.
DR   OrthoDB; 987250at2759; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000006790; Chromosome 4.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR   CDD; cd04263; DUF619-NAGK-FABP; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00150; ArgC_type1; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR000706; AGPR_type-1.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041734; NAGK-fArgBP.
DR   InterPro; IPR011241; NAGK/NAGSA.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR   NCBIfam; TIGR00761; argB; 1.
DR   NCBIfam; TIGR01850; argC; 1.
DR   PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR   PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF04768; NAT; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF036440; ARG5-6; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01224; ARGC; 1.
DR   PROSITE; PS51731; GNAT_NAGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036440};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR036440};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036440};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006790};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          348..500
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51731"
FT   ACT_SITE        672
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   859 AA;  94666 MW;  5A008B9B38BCEFE2 CRC64;
     MLTSKLLSAT KGLWSTSRGV RIAISPSGIF IRHIYYFTGG RERIPKAARF ISNLNGVGSF
     GTRSTVIQLL NNIGSKREVE QYLKFFTSVS EQQFAIIKVG GAIISDDLPE LASCLAFLYH
     VGLYPIVLHG TGPQVNNRLE AEGIAPEYID GIRITDRKTM TIVRECFLEQ NLKLVTALEQ
     LGVRARPITS GVFTAEYLDK DKYKLVGNIT KVCRDPIEAS IKAGALPILT SFAETHFGQT
     LNVNADIAAG ALARVFEPLK IVYLNEKGGI INGETGEKVS VINLDEEFDD LIKQSWVKYG
     TKLKIKEIKD LLDHLPRSSS VAIINVQDLQ KELFTDSGAG TMIRKGYKLV NRFSLSEFPS
     IDALRKILES DPEIGSGKTS VASYLRDLEL SNFVAYSDEP LEVLAIVKKD HKVPKLEKFL
     CSQGGWLNNV ADNVFKAIRR DSPTLQWIVD EDDPNIAWYF DKSDGSYLKN GKVLFYYGVD
     DVNTVSEILN EFSKDISSPS QYSKHSSNVF ASSQSIRSYS SMPQRTSPRL KGTNETASRV
     ALIGARGYTG QNLITLIQNH PYLELAFVSS RQNKGKKLEG YTKADIIYDN LDVNDVKRLE
     SNGRVDVWVM ALPNGICKPF VDAIESVKGS SKIVDLSADY RFVPESTAAY GLPELNDRTK
     IASAKKIANP GCYATGAQLS IAPLLPYVAG TPTIFGISGY SGAGTTPSPK NDPAYLKDNL
     IPYSLTDHIH EREISTKLGL PVAFTPHVGS WFQGITLTVS VPIKKSFIAT QNIHSLYQQF
     YKDEPLIHIS QEPPLVRDIS GNHNVTIGGF KVNDAQDRVV LISTIDNLLK GAATQCLQNI
     NLCLGYGEYT GIPLTTHKT
//
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