ID F0RA75_CELLC Unreviewed; 455 AA.
AC F0RA75;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN OrderedLocusNames=Celly_1595 {ECO:0000313|EMBL:ADY29419.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29419.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY29419.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP002534; ADY29419.1; -; Genomic_DNA.
DR AlphaFoldDB; F0RA75; -.
DR STRING; 867900.Celly_1595; -.
DR KEGG; cly:Celly_1595; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_1_10; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07136; ALDH_YwdH-P39616; 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; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 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|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487}.
FT DOMAIN 9..425
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 207
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 241
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 455 AA; 50949 MW; E1EC33947FB80C38 CRC64;
MMEILQKQQT FFKSQQTKNI TYRKQALIKL KQEITKREAD ICDAIYADFK KPRFESMAAE
TQFVLAELNY VIKHLKKWAR PEKVSGALLN FPSSDWLYKE PYGTVLIVAP WNYPFQLAIA
PLIGAIAAGN TAVIKPSEIT PNTSKIIVEI ITAVFSDAYV AVVEGGVEVS KNLLAQKWDY
IFFTGSTKVG KIFYKNAAEH LTPITLELGG KNPAIVDTTA NIKLAAKRIV WGKFLNAGQT
CIATDYILVH KDVKDKLIIA LQKSIEDSYG KNIEDSSDYA RTVSKNHFNN LNDLLEGQEI
IFGGQTNAKD NYMAPTLVNE PSLDSKLMQG EIFGPILPII AYTTEEDIQK YVLNYGKPLA
TYVFSTNRKF QQKIITKYSF GGGAINDTVI HITNKKLPFG GVGSSGIGAY HGKTSFDTFT
HQKAIIKRAN WLEAPLRYPP YNLPLKLVEK VKHLF
//
