ID A0A3M6VQ97_9STRA Unreviewed; 708 AA.
AC A0A3M6VQ97;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Semialdehyde dehydrogenase NAD-binding domain-containing protein {ECO:0000259|SMART:SM00859};
GN ORFNames=DD237_002900 {ECO:0000313|EMBL:RQM18364.1}, DD238_007063
GN {ECO:0000313|EMBL:RMX68211.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX68211.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|Proteomes:UP000282087, ECO:0000313|Proteomes:UP000286097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R13 {ECO:0000313|EMBL:RQM18364.1,
RC ECO:0000313|Proteomes:UP000286097}, and R14
RC {ECO:0000313|EMBL:RMX68211.1, ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) 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}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007239}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000256|ARBA:ARBA00006830}.
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:RMX68211.1}.
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DR EMBL; QLLG01000095; RMX68211.1; -; Genomic_DNA.
DR EMBL; QKXF01000076; RQM18364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M6VQ97; -.
DR STRING; 542832.A0A3M6VQ97; -.
DR VEuPathDB; FungiDB:DD237_002900; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000282087; Unassembled WGS sequence.
DR Proteomes; UP000286097; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_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; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000282087};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 357..503
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 708 AA; 75753 MW; C3B111821A54CE49 CRC64;
MSRTAVRSSQ AAVIPSTAYR AMGAPLINVT KFSIATLQTR ALSSKASDDY ALNLAKVLAP
EATLNEFKEL YRTPGVKHTT VIKIGGEVII NELETLIESL RFMKDTGLFP ILVHGAGPQM
NDELNKQGVE PQYVGGNRVT DQKTLDIAQK IFIDTNATLV AALNKAGVSA KGITNGVIQA
DFKDKEVYGF VGEVHKIHSN PVQAAIDAGQ IPVLSCLGES ANGQTLNINA DVAARQLALS
LQPLKTIFVN AKGGWIEDDG TKLKTINMTK DYERMAARDY TGRQGTLLKL NEINTLLQGL
PSTSSVVLTS ASQLMREIVS KKSAGTTCTK GEKPAVASEK SSTKSSAIPR GPNGKYRVGL
LGARGYVGGE LIRVIGRHPE LELVCASSRA LAGKKVVKVA SAPPLNPHTK LPAKLVEDVK
LNIDPELEFC ELGLDGIATS PFGESVDVWV VALPNGYCED YATALNALPR KDKIIIDLSA
DQRFNSEWTY GLPEAPGGRT RLQGATHISN PGCYATGAQL GLMPLLGGKP EVSGKLINES
VPPHVFGVSG YSGAGTNPSK ANDLEVLTDN IIAYKSVNHI HEHEVSHQLG TPVRFMPHVA
PYFQGIHLTL SAQLADNGIV TSAKQAEELY QEFFMNEALV KVTSDIPLVK DNAYHPHVTV
GGFQLDSDTG RLVVIATIDN LLKGAATQAV QNINVALGID EYVGIKFK
//
