ID A0A166V903_9HYPO Unreviewed; 387 AA.
AC A0A166V903;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetylglutamate kinase {ECO:0000313|EMBL:OAA33404.1};
GN ORFNames=AAL_00869 {ECO:0000313|EMBL:OAA33404.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:OAA33404.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:OAA33404.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:OAA33404.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004862}.
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:OAA33404.1}.
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DR EMBL; AZGY01000001; OAA33404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166V903; -.
DR STRING; 1081109.A0A166V903; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000078544; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Kinase {ECO:0000313|EMBL:OAA33404.1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000078544};
KW Transferase {ECO:0000313|EMBL:OAA33404.1}.
FT DOMAIN 74..196
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
SQ SEQUENCE 387 AA; 41804 MW; C8D108DABAED4CD3 CRC64;
MLSSASVAAR AGGRRIARRC VSTLPAVGPS RCLTSRLTGF TVASVSRQQR GYVVTANPNP
PLGKKNATND TPSRIGLIGA RGFTGQALVE LLNKHPFMDL RHVSSRELAG KELEGYTKGK
IIYETLSPED IAQLDQDGKV DCWIMALPNG VCKPYVDALD QVNSKSVVVD LSADFRFDDN
WTYGLPELVK RSKIAQSKRI SNPGCYATGA QIGLGGALDL IEGMPVIFGC SGYSGAGSKP
NSRNNLEVLK NAIIPYSLVS HVHEREISHQ LNHEVAFVPH VAGWYRGITL TLNIPLRKEV
TSRDVRLMYQ DRYAGEKLIK VVGEPPLVSS ISGRHGVEIG GFAVDSSGKR MVVVVTIDNL
AKGASTQCLQ NMNLALGYGE YEGIPIV
//
