ID   D3P2K3_AZOS1            Unreviewed;       476 AA.
AC   D3P2K3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Aldehyde dehydrogenase (NAD+) {ECO:0000313|EMBL:BAI75023.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:BAI75023.1};
GN   OrderedLocusNames=AZL_b03600 {ECO:0000313|EMBL:BAI75023.1};
OS   Azospirillum sp. (strain B510).
OG   Plasmid pAB510b {ECO:0000313|EMBL:BAI75023.1,
OG   ECO:0000313|Proteomes:UP000002040}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75023.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI75023.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI75023.1,
RC   ECO:0000313|Proteomes:UP000002040};
RC   PLASMID=pAB510b {ECO:0000313|EMBL:BAI75023.1};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024149};
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DR   EMBL; AP010948; BAI75023.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3P2K3; -.
DR   KEGG; azl:AZL_b03600; -.
DR   HOGENOM; CLU_005391_0_2_5; -.
DR   Proteomes; UP000002040; Plasmid pAB510b.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   CDD; cd07138; ALDH_CddD_SSP0762; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAI75023.1}; Plasmid {ECO:0000313|EMBL:BAI75023.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT   DOMAIN          16..472
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   476 AA;  50458 MW;  B8585176D35CEB88 CRC64;
     MTIMVDTTRF YIDGKWVQPR GSRLIDVINP ATEEAVTQVA LGTSTDVDLA VAAARKAFES
     FSRTTPAERI DLLSAILAVY QRRIEEFGDA IRQEMGAPQG FACQVQAGIG VAHLAQTIET
     ARSFPFEEDR GFQRILREPV GVVGLITPWN WPINQITCKV GPAIAAGCTM VLKPSELAPL
     SAALFAEVIH EAGVPAGVFN LVHGDGPEVG QAISAHPDID MVSFTGSTRA GIAVAKMAAD
     TVKRVTQELG GKSPNIILAD ADLAKAVTRG VERCFGNSGQ SCNAPTRMLV PEALYEQVAE
     LAKQAAAKAV VGDPLDPATT HGPVSNGNQF RKIQSLIETG IAEGAELLVG GPGRPEGLER
     GYFVRPTIFG RVTPDMTIAR EEIFGPVLSI ITYKDEEEAI RIANDTVYGL AGYVQSGDPA
     HGAAVARRLR AGTIYVNDPA WSAAVPFGGY GQSGNGREYA EFGLAEFVEI KGVVGA
//