ID W8VZI4_9FLAO Unreviewed; 517 AA.
AC W8VZI4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN ORFNames=NMS_0622 {ECO:0000313|EMBL:BAO54631.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO54631.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO54631.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO54631.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
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; AP014548; BAO54631.1; -; Genomic_DNA.
DR RefSeq; WP_041495336.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VZI4; -.
DR STRING; 1454201.NMS_0622; -.
DR HOGENOM; CLU_005391_1_2_10; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000031760; Chromosome.
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 38..498
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 517 AA; 55567 MW; 62735BF6125A845B CRC64;
MSEIAKAFAI NDALKQLGVE KINKGTSTGN ENFGNGAEII SSSPVDGAEI ARVTTTTADD
YDKVVAAAQT AFKDWRLKPA PLRGEVVRQF GDELRRLKEP LGKLVSYEMG KSYQEGLGEV
QEMIDICDFA VGLSRQLHGL TMHSERPGHR MYEQYHPLGI VGIISAFNFP VAVWAWNTAL
AWVCGDVCIW KPSEKTPLTG IACQNIIAKV LKDNNLPEGI SCLVNGDYKV GEMMTTDKRV
PLISATGSTR MGKIVASKVG ERLGKSLLEL GGNNAIIVTP DADIKMTVIG AVFGAVGTAG
QRCTSTRRLI VHDSMYDKVK TAVVDAYKQL KIGNPLDENN HVGPLIDKDA VKGYQNALTK
VVEEGGKVIV EGGVLEGKGF ESGCYVKPAI AEAENSFEIV QHETFAPVLY LLKYSGNVEN
ALDLQNGVNQ GLSSAIMTNN LREAEHFLSV AGSDCGIANV NIGTSGAEIG GAFGGEKDTG
GGRESGSDAW KIYMRRQTNT INYTTELPLA QGIKFDL
//