ID A0A059APB2_EUCGR Unreviewed; 373 AA.
AC A0A059APB2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Semialdehyde dehydrogenase NAD-binding domain-containing protein {ECO:0000259|SMART:SM00859};
GN ORFNames=EUGRSUZ_I01182 {ECO:0000313|EMBL:KCW55255.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW55255.1};
RN [1] {ECO:0000313|EMBL:KCW55255.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW55255.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-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 3/4.
CC {ECO:0000256|ARBA:ARBA00004862}.
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DR EMBL; KK198761; KCW55255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059APB2; -.
DR EnsemblPlants; KCW55255; KCW55255; EUGRSUZ_I01182.
DR Gramene; KCW55255; KCW55255; EUGRSUZ_I01182.
DR UniPathway; UPA00068; UER00108.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR023013; AGPR_AS.
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.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 32..169
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 373 AA; 41204 MW; 983157481D94A9E4 CRC64;
MWSNKRLLVR ASIAPSPQIA WKKSEKLQKD VRVAVLGASG YTGSEIVRLL ANHPHFGITL
MTADRKAGQS LGSVFPHLIT QDLPDMVAVK DADFSEVDAV FCCLPHGTTQ EIIKGLPKNL
KIVDLSADFR LRDILEYEEW YGQPHQAPEL QKEAVYGLTE ISREDIRHAH LVANPGCYPT
SIQLPLVPLI RANLIQLKNI IIDSKSGVSG AGRGAKEANL YTEIAEGIHS YGITKHRHVP
EIEQGLSEAA RSKITVSFTP HLMPMSRGMQ STIYVEMPSG VTVDDLYEQL KVAYQDEEFV
VLLGKGNVPH TRHVRGSNYC LMNVFPDRIP GRAILISVID NLVKGASGQA VQNLNVMMGL
PENMGLKYLP LFP
//
