ID Q13R74_PARXL Unreviewed; 499 AA.
AC Q13R74;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN ORFNames=Bxe_B2578 {ECO:0000313|EMBL:ABE33415.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33415.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE33415.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE33415.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000271; ABE33415.1; -; Genomic_DNA.
DR RefSeq; WP_011490784.1; NZ_CP008762.1.
DR AlphaFoldDB; Q13R74; -.
DR STRING; 266265.Bxe_B2578; -.
DR KEGG; bxb:DR64_4911; -.
DR KEGG; bxe:Bxe_B2578; -.
DR PATRIC; fig|266265.5.peg.5124; -.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 6187633at2; -.
DR Proteomes; UP000001817; Chromosome 2.
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 CDD; cd07130; ALDH_F7_AASADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 18..477
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 499 AA; 52944 MW; AA6B8A4FAFA0DBDB CRC64;
MDASTILADL GIAHAAQAGD IAVHSPITGE LIGRVASNTV AEVDTALAQA KQAYTAWRNV
PAPRRGELVR LLGNRLREKK QALGSIITLE TGKILQEGMG EVQEMIDICD FAVGLSRQLY
GLTIASERPG HRMAETWHPV GTCVVISAFN FPAAVWSWNA ALALVCGNAV IWKPSEKTPL
TALAVNQILS EALQEFGDAP AGLTALINGG RDVGAKLVAD PRASIVSATG STEMGRTVGV
EVAKRFGRSL LELGGNNAGI VTQTADHELA MRGILFSAVG TAGQRCTSLR RLFVHESVYD
KTIERLKQLY SKVPIGNPLE KGTLMGPLID KQSYGRMQEA LQQATAEGGK VFGGERVEVK
GYEGGYYVRP AIVEMPSQTS VVLKETFAPI LYVLRYTDFA DAVEANNAAV HGLSSCVFTT
DLREAERFLS DSGSDCGIAN VNIGPSGAEI GGAFGGEKET GGGRESGSDA WKAYMRRATN
TVNYSSALPL AQGIDFNIG
//
