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Database: UniProt/TrEMBL
Entry: Q0B7J8_BURCM
LinkDB: Q0B7J8_BURCM
Original site: Q0B7J8_BURCM 
ID   Q0B7J8_BURCM            Unreviewed;       503 AA.
AC   Q0B7J8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Aldehyde dehydrogenase (Acceptor) {ECO:0000313|EMBL:ABI89875.1};
DE            EC=1.2.99.3 {ECO:0000313|EMBL:ABI89875.1};
GN   OrderedLocusNames=Bamb_4323 {ECO:0000313|EMBL:ABI89875.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI89875.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000441; ABI89875.1; -; Genomic_DNA.
DR   RefSeq; WP_011659308.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0B7J8; -.
DR   GeneID; 69546555; -.
DR   KEGG; bam:Bamb_4323; -.
DR   PATRIC; fig|339670.21.peg.4630; -.
DR   eggNOG; COG1012; Bacteria.
DR   Proteomes; UP000000662; Chromosome 2.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07114; ALDH_DhaS; 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   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:ABI89875.1}.
FT   DOMAIN          22..486
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   503 AA;  54535 MW;  1E714CEFAA4E8732 CRC64;
     MKTTVETLQH ARIGNFIDGR FVEPASGSYA PSYDPTTSTP WYEFAQSNAA DVDAAVRSAQ
     AALKNPAWRR MTQTERGKLV RRLGELVLEH ADALALLECR DNGKLLKEMR AQMRAIPDSY
     LYFAGMADKL QGDTIPVNKL DMLNFNLREP IGVVGMIIPW NSPLMMLTGT LAPCLAIGNT
     VVVKPSEHAT ASSLALAELA IEAGIPPGVF NVVTGDGATT GEALTRHPGV AKYVFTGSTV
     TGRKIAGNAA QNLVPCQMEL GGKSPHVVFG DVEIERAVNG VVSGIFAAAG QTCVAGSRCF
     VEASIYERFV EALVERTRRV RVGHPMHDDT DIGPLALATQ LDKVQRYVAS GVEEGARIAA
     GGRRPSSGAL AEGWYFEPTV MTQATNSMRF MQEEIFGPVV GVVPFQDEAE LMALANDTEY
     GLASGIWTRD IDRAMRFARD IDAGTVWINT YRSAAYMSSN GGLKHSGYGR RGGFEVMREF
     SRLKNVVLDY SGAMQDPFVI RLR
//
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