ID   DOEC_HALED              Reviewed;         493 AA.
AC   E1V7V8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase (Non-phosphorylating);
DE            EC=1.2.1.- {ECO:0000305|PubMed:20849449};
GN   Name=doeC {ECO:0000303|PubMed:20849449}; OrderedLocusNames=HELO_3662;
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
CC   -!- FUNCTION: Involved in the degradation of ectoine, which allows
CC       H.elongata to utilize ectoine as both a carbon and a nitrogen source
CC       for growth. Probably catalyzes the NAD(+)-dependent oxidation of L-
CC       aspartate-semialdehyde to L-aspartate. {ECO:0000269|PubMed:20849449}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate 4-semialdehyde + NAD(+) = 2 H(+) + L-
CC         aspartate + NADH; Xref=Rhea:RHEA:45764, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:537519;
CC         Evidence={ECO:0000305|PubMed:20849449};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45765;
CC         Evidence={ECO:0000305|PubMed:20849449};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       ectoine as sole carbon source. {ECO:0000269|PubMed:20849449}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; FN869568; CBV43546.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1V7V8; -.
DR   SMR; E1V7V8; -.
DR   STRING; 768066.HELO_3662; -.
DR   PRIDE; E1V7V8; -.
DR   EnsemblBacteria; CBV43546; CBV43546; HELO_3662.
DR   KEGG; hel:HELO_3662; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; TMKRLVM; -.
DR   BioCyc; MetaCyc:MON-20121; -.
DR   Proteomes; UP000008707; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0042400; P:ectoine catabolic process; IMP:UniProtKB.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..493
FT                   /note="Aspartate-semialdehyde dehydrogenase (Non-
FT                   phosphorylating)"
FT                   /id="PRO_0000428760"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        293
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         160..161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..187
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         237..238
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  53137 MW;  096D6E88F82BE2EB CRC64;
     MTLSNQLSDL RLFRQYAYID GKWTHGDAGR EEAVFDPATG EAIGHIPVLE VEQIRGAVDA
     AEAAFVQWRA LRADERCERL LAWYDLLQAN REDLATIMTL EQGKPLPDAR GEVEYGASFV
     RWFAEEGKRT FGDTIPSHIP NAALGTIKEP VGIAALITPW NFPLAMITRK AAAAMAAGCP
     VIVKPAHETP YSALALAELA ERAGIPAGVF NVVLGEAAEV SKLLCDDERI KALSFTGSTR
     VGRLLLEQSA NTVKRVSLEL GGNAPFIVGP DMDPREAAFA AVAAKFQTAG QDCLAANRIL
     VHESIHDAFV EQFAERMAAL TVGNGLESEV DLGPLIHGQA VEKASAIVDD ALSRGATLVA
     GDQREAPGPN FFMPTLLTGV TPEMQVWREE NFAPVAGITS YRDDDEVIEM ANDTEYGLAA
     YVYTHDIRRI WKLLRALEYG MVSVNSVKMT GPPVPFGGVK QSGLGREGGV TGIDEYLETK
     YYCLGALGSV SGS