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Database: UniProt
Entry: A0A0K1W0B3_9MOLU
LinkDB: A0A0K1W0B3_9MOLU
Original site: A0A0K1W0B3_9MOLU 
ID   A0A0K1W0B3_9MOLU        Unreviewed;       867 AA.
AC   A0A0K1W0B3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   Name=adhE {ECO:0000313|EMBL:AKX33750.1};
GN   ORFNames=SLITO_v1c00820 {ECO:0000313|EMBL:AKX33750.1};
OS   Spiroplasma litorale.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=216942 {ECO:0000313|EMBL:AKX33750.1, ECO:0000313|Proteomes:UP000067476};
RN   [1] {ECO:0000313|EMBL:AKX33750.1, ECO:0000313|Proteomes:UP000067476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN-1 {ECO:0000313|EMBL:AKX33750.1,
RC   ECO:0000313|Proteomes:UP000067476};
RX   PubMed=26430038;
RA   Lo W.S., Lai Y.C., Lien Y.W., Wang T.H., Kuo C.H.;
RT   "Complete Genome Sequence of Spiroplasma litorale TN-1T (DSM 21781), a
RT   Bacterium Isolated from a Green-Eyed Horsefly (Tabanus nigrovittatus).";
RL   Genome Announc. 3:e01116-15(2015).
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; CP012357; AKX33750.1; -; Genomic_DNA.
DR   RefSeq; WP_075057849.1; NZ_CP012357.1.
DR   AlphaFoldDB; A0A0K1W0B3; -.
DR   STRING; 216942.SLITO_v1c00820; -.
DR   KEGG; sll:SLITO_v1c00820; -.
DR   PATRIC; fig|216942.3.peg.82; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000067476; 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; 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:UP000067476}.
FT   DOMAIN          3..266
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          452..849
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   867 AA;  95883 MW;  9FF8A1B5CEDBFB38 CRC64;
     MKEFEDLFKK ARESFEEFSQ FTQEKVDYIF KKAALAANEN RIHLAKLAKE ETKMGIIEDK
     ILKNHYASEF IYNKYKDLKT VGTFYSNDPG GIDKVYEPIG VVGAVIPTTN PTSTAIFKCL
     LCIKTRNTII ISPHPGAKKS TIEAAKIVLE AAVKAGAPKN IIGWIENPSL EGTEYVMKNS
     DIILATGGPG MVKAAYSSGV PAIGVGAGNA PAIIDDSADL ELATSSIVQS NTFDNGVVCA
     TENSVVVLES VYDKVVSLFE KKNTYIVTKE EEKNKFRKAM FKEGKFGLLN SELVGRSALD
     VAKLVGIKVP ETTRFILVET ESTEYDEALV HEKLSTYASL YKAKDFDDAI KKSKNILKLG
     PGHTASLFIN RKSSIEKVEK FKTLNPGRLL INSPSSLGGV GDMYNFMLEP SLTLGCGTKG
     GNSYSQNVTP LNLLNVKSLV ERRENMQWLR LPERIYHKFG SLEVALEDLK DWNIKNVFIV
     TDKIINQLYG KRVTSKLDDL NIKYTIFDDV EPNPMLSTTL RGSKMLENIK ADAIIGIGGG
     SSMDAAKLMW LYYESEEEVD FKDLAVTFAD IRKRIVRYPN TGRKAKMICI PTTSGTGSEV
     TPFSVITDDK DHKKYPLADY SLTPNMAIID PSLTMTVPKG ATNAPALDAL THCLESYVSV
     MATEYTDSYA LQGAKNIIEY LPRAYKDGAT DKEAREKVMN GAAFAGLSFA NAFLGIVHSL
     SHKIGGYHNV IHGAANAILL PYVIRYNAAC VLEGGKQGYF SQYETQNSME KYASLAKFIG
     LKGKSDEELV DALIDKVRAL TKEVELKTNF KDYGVDEKAF LNTLDKMSED AFDDQCTGAN
     PRYPLIEDIK QLYMDAYYGK DIKKFSK
//
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