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Database: UniProt
Entry: C7QZE3_JONDD
LinkDB: C7QZE3_JONDD
Original site: C7QZE3_JONDD 
ID   C7QZE3_JONDD            Unreviewed;       920 AA.
AC   C7QZE3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   OrderedLocusNames=Jden_1798 {ECO:0000313|EMBL:ACV09441.1};
OS   Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS   55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS   denitrificans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Jonesia.
OX   NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV09441.1, ECO:0000313|Proteomes:UP000000628};
RN   [1] {ECO:0000313|EMBL:ACV09441.1, ECO:0000313|Proteomes:UP000000628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC   NBRC 15587 / NCTC 10816 / Prevot 55134
RC   {ECO:0000313|Proteomes:UP000000628};
RX   PubMed=21304666; DOI=10.4056/sigs.41646;
RA   Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA   Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Han C.;
RT   "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT   55134).";
RL   Stand. Genomic Sci. 1:262-269(2009).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC       alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC       ECO:0000256|PIRNR:PIRNR000111}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC       ECO:0000256|PIRNR:PIRNR000111}.
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DR   EMBL; CP001706; ACV09441.1; -; Genomic_DNA.
DR   RefSeq; WP_015772069.1; NC_013174.1.
DR   AlphaFoldDB; C7QZE3; -.
DR   STRING; 471856.Jden_1798; -.
DR   KEGG; jde:Jden_1798; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_1_0_11; -.
DR   OrthoDB; 323926at2; -.
DR   Proteomes; UP000000628; Chromosome.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   CDD; cd08178; AAD_C; 1.
DR   CDD; cd07122; ALDH_F20_ACDH; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR034789; AAD_C.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012079; Bifunc_Ald-ADH.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000111; ALDH_ADH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000628}.
FT   DOMAIN          9..413
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          469..868
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   REGION          901..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  99215 MW;  8DEA3913EB9F3DE3 CRC64;
     MTATENAVAT PAQQEVDALV TKAQGALKEF LALDQEAVDY IVKKASVAAL SVHGELAVSA
     VKETGRGVFE DKAVKNIFAC EHVTNSMLSL RTAGVISHDE LTGITEIAEP VGVICGVTPV
     TNPTSTAIFK ALISLKTRNP IVFGFHPSAQ NCSVEAAKVV RDAAVAAGAP EDCIQWVEHP
     SLEATSALMN HPGVALILAT GGNAMVRAAY SCGKPALGVG AGNVPAFIER TARLKRAVND
     VVLSKAFDNG MICASEQAVI LDEPIYDEAM AEFRKLHAHV ATPAEKKMLE EFIFGVNANS
     ENCGEAKLNA TVVGKSPVWI AEQAGFEVPE DTSIILAEIS EVGPSEPLSR EKLSPVLAVL
     RAKDAEEGIR LSEQMVEFDG LGHSGAIHSD DQDIIREFGK RVKAVRIITN APSALGGIGD
     IYNAFIPSLT LGCGSYGHNS VSNNVSAVNL VNVKRIGRRN NNLQWFKVPA KTYFEPNAIR
     YLADMRGINR VTIVTDPTMT KLGFVDRILD VLHRRPGNRI ALQIIDNVMP EPTVKFVQEG
     AAQMRHFQPD TIIALGGGSP MDAAKVMWLL YEHPDIEFSD MKEKFFDVRK RAFKFPDLGA
     LAKLVCIPTT SGTGSEMTPF AVISDPEKNK KYPLADYALT PTVAIVDPVL TEMMPDFLAA
     DTGFDALTHA TEAYVSVYAN DYTDGLALHA IKLIFDNIVL SVKGGPGSKD EKVVKAREKM
     HNAGAIAGMA FGNAFLGIVH AMSHVTGSTF KLVHGRTNAT YLPHVIRYNG TVPTKLNAWP
     KYEHYVAPER FQQIAAHLGL PASTPEEGVE SYARAIEELR EAVGIPASFQ LQGVNEEAFI
     GRLDEVAMGA YEDQCAPANP RMPMIEDMKT IMEAAYYGTS FDEVRARRKA ARAAEVAVAK
     EETGDVAAPV DEPKARGKRK
//
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