ID A0A0P9IT58_RHOGW Unreviewed; 654 AA.
AC A0A0P9IT58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51731};
GN ORFNames=RHOBADRAFT_66897 {ECO:0000313|EMBL:KPV72561.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV72561.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV72561.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV72561.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004828}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR EMBL; KQ474086; KPV72561.1; -; Genomic_DNA.
DR RefSeq; XP_018268610.1; XM_018419117.1.
DR AlphaFoldDB; A0A0P9IT58; -.
DR STRING; 578459.A0A0P9IT58; -.
DR GeneID; 28979563; -.
DR OMA; GSKATIC; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041734; NAGK-fArgBP.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR NCBIfam; TIGR00761; argB; 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 SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 300..456
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 71729 MW; 3F17F2E3D0ED9491 CRC64;
MAKRWLGNAV AHSTDADRET IIRLLYSLAS RREVSRYLQI FSSATHFAVL KVGGAIITND
LESLTLSLNF LHRVGLYPVV VHGMGDKLNA RLEADGIVPD YIDGIRITDA RTLSHARRVF
LSENLKLVST LEELGTRARP ITGGVFTAEY LDEARYGYVG RITSVDKEPI EASIRAGALP
ILTSLAETPE GQILNVNADV ATAELSKVLE PLKIVYLSEK GGLYHGVTKE KLSLINLDEE
YDDLMKQDWV KYGTKLKLRE IKELLDHLPR ASSVAIISPD NLQKELFTDS GAGTLLRRGY
KLYKHTSIEG VGQDRLRRVL AERDEDVTSG RKSVAQVLSE LEKSHAPFTI YGDEPCDVVA
IVSHPEGQVP VMTKFLANQN AIQNGVTDNV FNSVRKDFKR LFWTAKADDE NKAWHFERAD
GSFTRNGRSL FYYGVQDAGE VERLVKDLDA AGRVERSYLP ISYTSSSRGT VSSPGNLASA
FNTRSYSTRA RPAAASSSSS PSSSPFGQSQ QARSFSSSPS YAATAKRVAL IGARGYTGQN
LVSLINSHPS FELAHVSSRE LAGQPLDGYT KSSVTYENLG YKEIEQLEQR GDVDAWVMAL
PNGVMAPFVD AIDKGCANKP ESKKSVVIDL GADKRFDESW TYGLPGESLV AASA
//
