ID   A0A066UK11_9VIBR        Unreviewed;       372 AA.
AC   A0A066UK11;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   29-APR-2015, entry version 6.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004501};
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|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004501};
DE   AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
GN   Name=asd {ECO:0000256|HAMAP-Rule:MF_02121};
GN   ORFNames=VFDL14_01900 {ECO:0000313|EMBL:KDN27756.1};
OS   Vibrio fortis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN27756.1};
RN   [1] {ECO:0000313|EMBL:KDN27756.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Dalian14 {ECO:0000313|EMBL:KDN27756.1};
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.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC       semialdehyde (L-ASA) by the reductive dephosphorylation of L-
CC       aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate +
CC       NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000256|HAMAP-
CC       Rule:MF_02121, ECO:0000256|RuleBase:RU004501}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC       {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004502}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 2/3.
CC       {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004502}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_02121, ECO:0000256|RuleBase:RU004502}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_02121,
CC       ECO:0000256|RuleBase:RU004041}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KDN27756.1}.
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DR   EMBL; JFFR01000025; KDN27756.1; -; Genomic_DNA.
DR   RefSeq; WP_032551976.1; NZ_JFFR01000025.1.
DR   EnsemblBacteria; KDN27756; KDN27756; VFDL14_01900.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
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   TIGRFAMs; TIGR01745; asd_gamma; 1.
DR   PROSITE; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121,
KW   ECO:0000256|RuleBase:RU004501};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004501};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121,
KW   ECO:0000256|RuleBase:RU004501};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND       9     12       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND      36     37       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND     165    166       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    135    135       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02121,
FT                                ECO:0000256|PIRSR:PIRSR000148-1}.
FT   ACT_SITE    275    275       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121, ECO:0000256|PIRSR:PIRSR000148-
FT                                1}.
FT   BINDING      73     73       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   BINDING     102    102       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     193    193       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   BINDING     241    241       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     244    244       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     268    268       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     351    351       NADP. {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
//