ID   A0A066UK11_9VIBR        Unreviewed;       372 AA.
AC   A0A066UK11;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   13-SEP-2023, entry version 34.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120, ECO:0000256|HAMAP-Rule:MF_02121};
DE            Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
DE            Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121};
DE            EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120, ECO:0000256|HAMAP-Rule:MF_02121};
DE   AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
GN   Name=asd {ECO:0000256|HAMAP-Rule:MF_02121,
GN   ECO:0000313|EMBL:KAB0290200.1};
GN   ORFNames=F2P58_04520 {ECO:0000313|EMBL:KAB0290200.1}, F2Z80_03915
GN   {ECO:0000313|EMBL:KAB0303155.1}, VFDL14_01900
GN   {ECO:0000313|EMBL:KDN27756.1};
OS   Vibrio fortis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN27756.1, ECO:0000313|Proteomes:UP000027219};
RN   [1] {ECO:0000313|EMBL:KDN27756.1, ECO:0000313|Proteomes:UP000027219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dalian14 {ECO:0000313|EMBL:KDN27756.1,
RC   ECO:0000313|Proteomes:UP000027219};
RA   Wang Y., Song L., Liu G., Ding J.;
RT   "Vibrio fortis Dalian14 Genome Sequencing.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAB0303155.1, ECO:0000313|Proteomes:UP000326687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S7-72 {ECO:0000313|EMBL:KAB0303155.1,
RC   ECO:0000313|Proteomes:UP000326687};
RA   Das S.K.;
RT   "Vibrio Fortis S7-72.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAB0290200.1, ECO:0000313|Proteomes:UP000326789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AN60 {ECO:0000313|EMBL:KAB0290200.1,
RC   ECO:0000313|Proteomes:UP000326789};
RA   Das S.K.;
RT   "Whole genome sequence of Vibrio fortis.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC       semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-
CC       4-phosphate. {ECO:0000256|ARBA:ARBA00002492, ECO:0000256|HAMAP-
CC       Rule:MF_02121}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_02121};
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, ECO:0000256|HAMAP-Rule:MF_02121}.
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, ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097,
CC       ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_02121}.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010584, ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}.
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:KDN27756.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; VWSE01000003; KAB0290200.1; -; Genomic_DNA.
DR   EMBL; VXDD01000001; KAB0303155.1; -; Genomic_DNA.
DR   EMBL; JFFR01000025; KDN27756.1; -; Genomic_DNA.
DR   RefSeq; WP_032551976.1; NZ_VXDD01000001.1.
DR   AlphaFoldDB; A0A066UK11; -.
DR   STRING; 212667.VFDL14_01900; -.
DR   EnsemblBacteria; KDN27756; KDN27756; VFDL14_01900.
DR   OrthoDB; 9022717at2; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000027219; Unassembled WGS sequence.
DR   Proteomes; UP000326687; Unassembled WGS sequence.
DR   Proteomes; UP000326789; Unassembled WGS sequence.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_02121; ASADH; 1.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR011534; Asp_ADH_gamma-type.
DR   InterPro; IPR012080; Asp_semialdehyde_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   NCBIfam; TIGR01745; asd_gamma; 1.
DR   PANTHER; PTHR46278:SF4; 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.
DR   PROSITE; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW   ECO:0000256|HAMAP-Rule:MF_02121};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_02121};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_02121}; NADP {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121,
KW   ECO:0000313|EMBL:KDN27756.1};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW   Rule:MF_02121}.
FT   DOMAIN          2..122
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        135
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   ACT_SITE        275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         9..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         36..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         73
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         102
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         165..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         244
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT   BINDING         351
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
SQ   SEQUENCE   372 AA;  40359 MW;  ADB9DEB581265CC6 CRC64;
     MRVGLVGWRG MVGSVLMQRM VEERDFDLIE PVYYSTSQIG IPAPVLGGKD AGLLQDAFDI
     DSLKQLDAVI TCQGGDYTSK VYPALRQAGW KGYWIDAAST LRMDADSIIT LDPVNLAQIQ
     QGIHGGTNTF VGGNCTVSLM LMALGGLYEK GMVEWMSAMT YQAASGAGAK NMRELISQMG
     VINDSVSSEL ANPASSILDI DKKVADTIRS ESFPTDQFGA PLAGSLIPWI DVKRENGQSK
     EEWKAGVEAN KILGLDGQPI PIDGTCVRIG AMRCHAQALT IKLKQDVPMD EIEEIIATHN
     DWVKVIPNDR DITAQELTPA KVTGTMSVPV GRLRKMSMGN DFLNAFTVGD QLLWGAAEPL
     RRTLRIILAE KA
//