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
//