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Database: UniProt
Entry: A0A0A1M9V4_9BACI
LinkDB: A0A0A1M9V4_9BACI
Original site: A0A0A1M9V4_9BACI 
ID   A0A0A1M9V4_9BACI        Unreviewed;       475 AA.
AC   A0A0A1M9V4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Glutarate-semialdehyde dehydrogenase DavD {ECO:0000313|EMBL:CEI82125.1};
GN   Name=davD {ECO:0000313|EMBL:CEI82125.1};
GN   ORFNames=BN997_01983 {ECO:0000313|EMBL:CEI82125.1};
OS   Oceanobacillus oncorhynchi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI82125.1, ECO:0000313|Proteomes:UP000040453};
RN   [1] {ECO:0000313|EMBL:CEI82125.1, ECO:0000313|Proteomes:UP000040453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oc5 {ECO:0000313|EMBL:CEI82125.1,
RC   ECO:0000313|Proteomes:UP000040453};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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DR   EMBL; CDGG01000001; CEI82125.1; -; Genomic_DNA.
DR   RefSeq; WP_042531728.1; NZ_CDGG01000001.1.
DR   AlphaFoldDB; A0A0A1M9V4; -.
DR   STRING; 545501.BN997_01983; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000040453; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR42991; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42991:SF1; ALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000040453}.
FT   DOMAIN          16..469
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   475 AA;  51253 MW;  AF647A7E02114B11 CRC64;
     MQSSILKEKL FINGEWIETE GTHQVFNKYT GELFSEIALA DEKIVDQVIN AAVTAHKEIN
     FPVEQRYEVL MRAADLLKQN QTALAETIAI EGGKPISDAN VEVTRSVSTL QVAAEEAKKL
     TGEIIPNYNA PGRFLYTVKK PVGVVAAITP FNFPLNLVVH KVGPALAAGN PIIIKPASDT
     ATTTVKLCEL LEEAGVPKGY VQCVVGSGRT VGEQLLNDER IVHYTFTGSP AIGKHIQQTI
     GLRKATLELG SNSATIVHHD TDVEKAAKKI ARMANVNAGQ VCISVQRVFI HDSIKEAFLD
     TLVREVAQLK VGDPLNKDTN VGPMISEKEA RRIESWIDEA VSAGAVVLTG GKREGSVVQP
     AVLTNVKKGM KIVDEEAFAP IVSVSSYDTI EEAVALVNDS KYGLQAGIYT SDLKLSYQIP
     YLLEVGGVII NDTSSFRADQ MPYGGVKESG NGKEGPAYAI QELVETVTVV VNLEE
//
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