ID Q13FK5_PARXL Unreviewed; 798 AA.
AC Q13FK5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:ABE37134.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:ABE37134.1};
GN ORFNames=Bxe_C1274 {ECO:0000313|EMBL:ABE37134.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE37134.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE37134.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE37134.1,
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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036490, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000272; ABE37134.1; -; Genomic_DNA.
DR RefSeq; WP_011494360.1; NZ_CP008761.1.
DR AlphaFoldDB; Q13FK5; -.
DR STRING; 266265.Bxe_C1274; -.
DR KEGG; bxb:DR64_8539; -.
DR KEGG; bxe:Bxe_C1274; -.
DR PATRIC; fig|266265.5.peg.9025; -.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 6187633at2; -.
DR Proteomes; UP000001817; Chromosome 3.
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; cd07111; ALDH_F16; 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; IPR011408; Aldehyde_DH.
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; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; ALDH-like; 2.
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 41..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 541..765
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 798 AA; 85677 MW; A670D297C41B61FE CRC64;
MSVAEYFSSM EYGPAPESDQ AARAWLAQHE ARFGHFIGGA WREPGAGERF ASHAPASGEP
LAQIAHGDAG DIDAAVCAAR AAQPAWLALG GAGRARHLYA LARMVQRHSR LFAVLEALDN
GKPIRETRDI DVPLVARHFL HHAGWAQLQE SEFAAYAPLG VIGQIVPWNF PLLMLAWKIA
PAIAMGNCVV LKPAEYTPLT ALLFAELAHR AGLPAGVLNV VTGDGRTGAA LVEHPQIDKI
AFTGSTEVGK AIRAVTAGSG KSLTLELGGK SPFIVFDDAD LDGAVEGVVD AIWFNQGQVC
CAGSRLLVQE GIEARFIARL KRRMETLRIG SSLDKSIDIG AIVDPVQLER IRSLVETGRR
EGCAVWQSPG TVLPAQGCFY PPTLVTGVAP ASTLAQQEIF GPVLVAMSFR TPDEAIALAN
NSRYGLAASV WSETIGRALD IAPRLACGVV WINATNLFDA AVGFGGYRES GYGREGGREG
IYEYLKPRAW LNLGWRQPRN AETVADQPER SLNVMAIDRV DRTAKLFIGG KQVRPDSGYS
LPVYAPDGTP VGEVGEGNRK DIRNAVEAAR AAHKWSQASA HNRAQVLFYL AENLSVRADE
FARQLMQRNG ATEAVARAEV EASVTRLFTY AAWADKFDGA VHTPPLRGVA LAMHEPLGVI
GIACPDEAPL LGFVSLMAPA LAMGNRVIVL PGQACPLAVT DFYQVAETSD VPGGVLNVIT
GERGALLPAL ARHNDVDALW CFGSAADSTL VERESAGNLK RTFTDYGRQF DWFDPSSEGL
PFLREAVQVK NIWVPYGD
//