ID Q63NJ2_BURPS Unreviewed; 470 AA.
AC Q63NJ2;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:CAH37755.1};
GN OrderedLocusNames=BPSS0307 {ECO:0000313|EMBL:CAH37755.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH37755.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH37755.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH37755.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; BX571966; CAH37755.1; -; Genomic_DNA.
DR RefSeq; WP_011205384.1; NZ_CP009537.1.
DR RefSeq; YP_110327.1; NC_006351.1.
DR AlphaFoldDB; Q63NJ2; -.
DR STRING; 272560.BPSS0307; -.
DR KEGG; bps:BPSS0307; -.
DR PATRIC; fig|272560.51.peg.6413; -.
DR eggNOG; COG1012; Bacteria.
DR Proteomes; UP000000605; 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; cd07092; ALDH_ABALDH-YdcW; 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 InterPro; IPR015657; Aminobutyraldehyde_DH.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF307; GAMMA-AMINOBUTYRALDEHYDE DEHYDROGENASE; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT DOMAIN 13..466
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 470 AA; 49429 MW; 4488BFD99653902C CRC64;
MLINGLCIEG GGEPLPIVDP ATGEPLAAPA AASAADLERA VAAAEAAFPA WRATTPATRA
SLLLALADEI DRQAGALARI ESRNTGKPLH LVVQDELPAV ADCFRFYAGA ARTASGPSAG
EYVEGHTSMV RRDPVGVVAQ IAPWNYPLMM AAWKLAPALA AGNTIVFKPS EWTPLSIVAL
EAALARIFPA GVVNIVLGDG ASVGRALATH PRVRMISLTG SVEAGKSVLA AAACNLKRTH
LELGGKAPVL VFDDADLDAA VAGIRYAGFY NAGQDCTAAT RIYVQRGIYD TLAQRLADAA
STLRVGPPDR ADAEMGPLVS AAHRARVERF VREAAALRHA RVLTGGAPLP GPGCYYAPTV
IAGVRHDDAP MRREAFGPVV TLTPFDTESQ ALRWANDSEY GLASSVWTRD AARGMRLAAC
IDAGVTWVNA HFTYTADMPH GGTKQSGYGS DLSTLGLADY TQPRHVMWRH
//
