ID A5FAQ7_FLAJ1 Unreviewed; 442 AA.
AC A5FAQ7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN OrderedLocusNames=Fjoh_4713 {ECO:0000313|EMBL:ABQ07712.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ07712.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ07712.1, ECO:0000313|Proteomes:UP000006694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC UW101 {ECO:0000313|Proteomes:UP000006694};
RX PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ07712.1; -; Genomic_DNA.
DR RefSeq; WP_012026678.1; NZ_MUGZ01000004.1.
DR AlphaFoldDB; A5FAQ7; -.
DR STRING; 376686.Fjoh_4713; -.
DR KEGG; fjo:Fjoh_4713; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_1_10; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000006694; 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}.
FT DOMAIN 8..411
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 194
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 228
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 442 AA; 50097 MW; 134DC6513218F20A CRC64;
MDFKNDIGYR KETLKKLLYN IQKNEDLIVK ALYDDFKKPE FEAVLTETNY VISELKDTIK
NINSWAKPKR VLPSILNFPS SDYIYKEPYG NVLVIAPWNY PFQLALCPLI AAVAAGNRVV
LKPSELTPHT SSIIAKLIEK TFHISHVEVF EGGVEVSNKL LAERWDYIFF TGSVSVGKII
AKAAAENLTP VTLELGGKNP CVIDETANLK LAAKRIVWGK FINAGQTCIA PDYILIQKNM
KVNFISFLME EIVNAYGKKI DKSPDFARII NTKNWVRLDQ MIEREKVIFG GETNHDKLYI
SPTLIEEPSL DSPVMKEEIF GPILPILTYE TEAEIHNVIS KYEKPLAFYI FSENKSFTKK
LISNYAFGGG CINDTVVHFS NKRLPFGGVG HSGIGAYHGQ MSFDTFSHHK AIVKKGNWLD
LPMRYAPYKD KLTSIKRILD WI
//
