ID   A0A231PLQ2_9ACTN        Unreviewed;       880 AA.
AC   A0A231PLQ2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=CHR28_09175 {ECO:0000313|EMBL:OXS35592.1};
OS   Streptomyces sp. XY006.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2021410 {ECO:0000313|EMBL:OXS35592.1, ECO:0000313|Proteomes:UP000215527};
RN   [1] {ECO:0000313|EMBL:OXS35592.1, ECO:0000313|Proteomes:UP000215527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XY006 {ECO:0000313|EMBL:OXS35592.1,
RC   ECO:0000313|Proteomes:UP000215527};
RA   Shan W., Liu H., Zhou Y., Yu X.;
RT   "Draft Genome Sequence of Streptomyces sp. XY006, an Endophyte Isolated
RT   from Tea (Camellia sinensis).";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXS35592.1}.
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DR   EMBL; NOKT01000006; OXS35592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231PLQ2; -.
DR   OrthoDB; 323926at2; -.
DR   Proteomes; UP000215527; Unassembled WGS sequence.
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}.
FT   DOMAIN          9..288
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          477..869
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   880 AA;  94543 MW;  1B7E7E4111C6BE58 CRC64;
     MTRQDTRAKE RVGTDAPSDT AVAVDRLVTA GLKALADYEA FSQEQVDHIV KKASVAALDQ
     HTALARLAVE ETGRGVFEDK AAKNMFACEH VTHSMGHMKT VGVVGRDDIE DMVEIAEPVG
     VVAAVTPVTN PTSTTIFKAL MALKTRNPVI FAFHPSAQQC STEAARVVRD AAVAAGAPEH
     CVQWIEAPSV EATRTLMRHA GVSLILATGG NAMVKAAYSA GKPALGVGAG NVPAYVHRSA
     KLRRAVNDLV LSKSFDNGMI CASEQAVILD TEIYDAAITE FHALHAHLAT PDEKVKLETF
     LFPTTGGSGA GCEPKVNAAA VGRSPAWIAE RAGFSVPADT SVILVEAERV GPDEPLTREK
     LCPVLAVLRA EDELRGFDLA ADMVAFHGQG HSAVIHTEDA AVAEAYGTRM KTVRIIVNSP
     SSQGAIGGVY NGLLPSLTLG CGSWGSTSVS NNVSAAQLLN IKRVSTRRNN LQWFKVPPKI
     YFEPQAIRYL TSMPDVHRVT IVTDATMTRL GFVDRISRVL QRRREPVTLQ IIDNVRPEPS
     IDSVQHGADL MRDFRPDTII ALGGGSPMDA AKVMWLLYEQ PGIDFTDMRQ KFSDIRKRAF
     RFPTLGKQAR LVCVPTTSGT GAEVTPFAVI SDPATGKKYP LADYALTPSV AIIDPLLTTA
     LPPALAADSG FDALTHAIEA YVSVYANDFT DGLALHAIRL VFGHLEAAVN NHATAAEARE
     KMHNAGTIAG MAFGNAFLGI VHAMSHTLGA TFRIAHGRTN AVLLPHVIRY NGTIPTKLTG
     WPKYENYRAP ERFQDIARTL GLPAATPAEG VQSLASAVER LRDTVGIEPT FQALGIDERA
     FLDALPQQAL NAYEDQCAPA NPRMPMLDDM QELMRTAYHG
//