ID A0A329RJE6_9STRA Unreviewed; 391 AA.
AC A0A329RJE6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN ORFNames=JG687_00010875 {ECO:0000313|EMBL:KAG6955948.1}, PC110_g18817
GN {ECO:0000313|EMBL:RAW24754.1}, PC113_g17481
GN {ECO:0000313|EMBL:KAG2848982.1}, PC117_g18505
GN {ECO:0000313|EMBL:KAG2913810.1}, PC129_g15908
GN {ECO:0000313|EMBL:KAG3213149.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW24754.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW24754.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW24754.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG2848982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15-7 {ECO:0000313|EMBL:KAG2848982.1}, 4040
RC {ECO:0000313|EMBL:KAG2913810.1}, and P421
RC {ECO:0000313|EMBL:KAG3213149.1};
RA Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT "Effector identification in a new, highly contiguous assembly of the
RT strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG6955948.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 3830 {ECO:0000313|EMBL:KAG6955948.1};
RA Mcdougal R., Panda P., Williams N., Studholme D.J.;
RT "Phytophthora aleatoria, a newly-described species from Pinus radiata is
RT distinct from Phytophthora cactorum isolates based on comparative
RT genomics.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001636};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00005076}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005021}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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:RAW24754.1}.
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DR EMBL; RCMG01000757; KAG2848982.1; -; Genomic_DNA.
DR EMBL; RCMK01000750; KAG2913810.1; -; Genomic_DNA.
DR EMBL; RCMV01000764; KAG3213149.1; -; Genomic_DNA.
DR EMBL; JAENGZ010000636; KAG6955948.1; -; Genomic_DNA.
DR EMBL; MJFZ01000838; RAW24754.1; -; Genomic_DNA.
DR STRING; 29920.A0A329RJE6; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR Proteomes; UP000688947; Unassembled WGS sequence.
DR Proteomes; UP000735874; Unassembled WGS sequence.
DR Proteomes; UP000736787; Unassembled WGS sequence.
DR Proteomes; UP000760860; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02121; ASADH; 1.
DR InterPro; IPR012080; Asp_semialdehyde_DH.
DR InterPro; IPR005986; Asp_semialdehyde_DH_beta.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR01296; asd_B; 1.
DR PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR PIRSF; PIRSF000148; ASA_dh; 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:ARBA00023167};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000251314};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..125
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 139
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 391 AA; 41965 MW; 72DBDE6C3842A2CA CRC64;
MTTPNGKTIG ICGATGAVGI EIISVLAAHK FPVKQLVLFA SSRSAGKKVD TAFGEVAISL
FSVEKAAKLD YVFLAVSGDF SLQYAKELAA VPNGPVVIDN SSAFRRHPEI PLVIPEINGH
VLIQKDGKPQ PKLIANPNCT TAIAAMALWP LHCEFGIKKL IVSTYQAASG AGAAGMEELA
DGAKAFLADE PVTYKVFSYP LPFNLIPHID KFQENGYTKE EMKVTWETRK IFGEPNLAVS
CTAARIPIMR AHSEALSIET VKPVNIARAR EILAKADGVD LVDEPEKLLY PMPKNATKKF
NIEAGRLRKS LVFGDHGLEL FVSGDQLLRG AALNAVLIAE FLENPRSTPQ FTKKPTTCSL
SKDQQQVVLG LVAGVAVSAA SVLAYGLVKK N
//
