ID   E4RU30_LEAB4            Unreviewed;       780 AA.
AC   E4RU30;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:ADQ16011.1};
GN   OrderedLocusNames=Lbys_0218 {ECO:0000313|EMBL:ADQ16011.1};
OS   Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS   106382 / 4M15).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Leadbetterella.
OX   NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ16011.1, ECO:0000313|Proteomes:UP000007435};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Leadbetterella byssophila DSM 17132.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ16011.1, ECO:0000313|Proteomes:UP000007435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC   {ECO:0000313|Proteomes:UP000007435};
RX   PubMed=21475582; DOI=10.4056/sigs.1413518;
RA   Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA   Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Leadbetterella byssophila type strain
RT   (4M15).";
RL   Stand. Genomic Sci. 4:2-12(2011).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR036490, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP002305; ADQ16011.1; -; Genomic_DNA.
DR   RefSeq; WP_013407066.1; NC_014655.1.
DR   AlphaFoldDB; E4RU30; -.
DR   STRING; 649349.Lbys_0218; -.
DR   KEGG; lby:Lbys_0218; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_018339_0_0_10; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000007435; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007435}.
FT   DOMAIN          41..486
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          524..750
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   780 AA;  85987 MW;  346EDB7AE2195D51 CRC64;
     MNVKDIFLTM EYGPAPESDK NAQEFLDQHD RRFGLFINGE WTEGENHFPS LNPATGETLA
     QISEASTAQV EAAVAAAKSA YPSWSQLSGH ERAKYLYALA RQIQKHSRLF AVLETLDNGK
     PIRETRDIDI PLVARHFYHH AGWAQVMEQE FPNFESIGVI GQIVPWNFPL LMLSWKIAPA
     LAMGNTLVLK PAEQTSLTAL LFAEICQEIG LPKGVVNIIT GHGSVGEALT LHPDVQKIAF
     TGSTEVGKKI RRNTAGSSKK LSLELGGKSP FIVFEDADLD STVEGIVDAI WFNQGQVCCA
     GSRLLVQESI AEKFYAKIKN RIQKLVLGSP LDKGIDMGAL VSEEQWNTVN GFVERAKAEG
     LEYWQVENCP TKGCYFPPTL FPYVSPASEI AQEEIFGPVL VGMTFRSHQE AIKLANNTRY
     GLAASLWTEN INLALDVAPQ IKAGTVWINT TNVFDAASGF GGYRESGFGR EGGKEGLYEY
     IKPKSIKSST GFTIHNKEVN LRSYIDRTPK MYIGGKQARP DSGYSIKVSN PAGQTVGEVG
     EGTRKDIRNA VEAAHAQSGW AGMTGHARAQ VLYFIAENLS ARAEEFEQRL VEASGYSGKD
     AKLEVEKSLE RIFTYAAYAD KFDGRVHSTT SRHVTIAMHE PVGILGVVCP KEYPLLGMIS
     LVLPAIAMGN RVIVLPSETS PLSTTDFYQI LDTSDVPGGT VNIITGDHKS LTTELAKHFD
     VDGIWYFSDK QNAETLEKLA ADSMKRTWIE SEYDWLQNPL QKVFLRKATE VKNIWIPYGA
//