ID S2JUJ6_MUCC1 Unreviewed; 847 AA.
AC S2JUJ6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51731};
GN ORFNames=HMPREF1544_09829 {ECO:0000313|EMBL:EPB83445.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB83445.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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; KE124071; EPB83445.1; -; Genomic_DNA.
DR AlphaFoldDB; S2JUJ6; -.
DR STRING; 1220926.S2JUJ6; -.
DR VEuPathDB; FungiDB:HMPREF1544_09829; -.
DR eggNOG; KOG2436; Eukaryota.
DR eggNOG; KOG4354; Eukaryota.
DR InParanoid; S2JUJ6; -.
DR OMA; IAFIPHV; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000014254; 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: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 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; 2.
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:UP000014254};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 337..500
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT ACT_SITE 662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 847 AA; 93135 MW; C5D5CBF203646B71 CRC64;
MLSIARKSTL SGNISRLAQR SVATATVRPI ALIPGQQLNQ RRNYTNANAT AEKETITKLL
YNIGSRKEVE QYLRHFSSVE SQKFAVIKVG GAVLTDELET LASALTFLNR VGLYPIVLHG
AGPQLNRLLE EAKVEPQYEE GIRITDPATL EIARKVFMAE NLKLVDALER HGTRARPIPG
GVFVADYLDK EKYGYVGKIT GVNKEVIESS IRAGALPILT SLAETPTGQI LNVNADVAAA
ELATVLEPLK IVFLNEKNGL YHGVTGKKID VINLDEEYED LLKEPWVRYG TKLKINQCKE
LLDGLPRSSS VAIISAGHLH KELFTDSGAG TLIRRGHKLF KYNKLDEVDP DKLRRIMEAE
DASIQAGEGS VASYLRSLQQ KDVQIYTDEP GQVLAIVTKD PKDPSKPAVL EKLLTSKTAV
LNNVPENLWN SIRKDNDALT WRVDGKAKEG NLDPSWHFER ADGSLKNSQD GSTTFFYGIA
DNDKIKQTLN SISSQKASVP SGARSYSTYR RNNFQFMSRR GFASAAGPKN VGLIGARGYT
GRELINLINS HPNLNLTHVS SRELEGKPLE GYTKADLTYV NLKPDDLKAQ KQVDAWVLAL
PNGVCTPFVK QINEDVKSGQ SSEKVLVDLS ADHRFDTTWT YGLPEFNREN LKGATRVANP
GCYATGAQMS LRPLLPFLDK HSAPTVFGVS GYSGAGTKPS LKNDPAFLKD NLIPYSLTNH
IHEREVSYQL GTSVNFIPHV ASWFQGIALT VNVPLNKTMS SQDIKSAFEE FYQGEQLVKV
LESGEPLVRD NAGKHFVRVG GFNVHPDGRR AVITTTIDNL LKGAATQAVQ NLNLSLGFDE
YAGIPTN
//
