ID   A0A2K2TUC8_9CLOT        Unreviewed;       870 AA.
AC   A0A2K2TUC8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=C0033_13290 {ECO:0000313|EMBL:PNV61552.1};
OS   Clostridium sp. chh4-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2067550 {ECO:0000313|EMBL:PNV61552.1, ECO:0000313|Proteomes:UP000236356};
RN   [1] {ECO:0000313|Proteomes:UP000236356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=chh4-2 {ECO:0000313|Proteomes:UP000236356};
RA   Huang C.-H.;
RT   "Clostridium sp. nov. strain chh-4-2., isolated from the gut of a healthy
RT   Taiwan adult.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PNV61552.1}.
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DR   EMBL; PKUU01000011; PNV61552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K2TUC8; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000236356; Unassembled WGS sequence.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1990362; F:butanol dehydrogenase activity; IEA:InterPro.
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; 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; IPR044731; BDH-like.
DR   InterPro; IPR012079; Bifunc_Ald-ADH.
DR   PANTHER; PTHR43633; ALCOHOL DEHYDROGENASE YQHD; 1.
DR   PANTHER; PTHR43633:SF1; ALCOHOL DEHYDROGENASE YQHD; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236356}.
FT   DOMAIN          21..275
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          464..855
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   870 AA;  94794 MW;  4EF6F53954E881CC CRC64;
     MANKTEVTVP AIIDSVDALI AKMKAMREAQ KIFATYTQEQ VDKIFYEAAK AANQMRIPLA
     KMAVEETGMG VVEDKVIKNN YAAEYIYNAY KNTKTCGVVE EDKAFGIKKI AEPIGLIAAV
     IPTTNPTSTA IFKTLISLKT RNAIIISPHP RAKGCTIAAA KVVLDAAVKA GAPEGIIGWI
     DVPSLELTNE VMRGADTILA TGGPGMVTAA YSSGKPALGV GAGNTPVIID DTADIKMAVN
     SIIHSKTFDN GMICASEQSV TVLESIYREV KKEFEYRGCY FLKADEIDKV RKTILINGAL
     NAKIVGQSAH KIASLAGVNV PVDTKILIGE VESVNIEEEF AHEKLSPVLA MYKAKTFDEA
     IAKAEQLVAD GGYGHTASLF INPNETEKMA KHAAAMKTCR IVINTPSSHG GIGDLYNFKM
     TPSLTLGCGS WGGNSVSENV GVKHLLNIKT VAERRENMLW FRQPEKVYFK KGCMPVALDE
     LGTVMGKKRA FIVTDSFLYM NGYTKPITDK LDEMGIVYQC FSEVQPDPTL ANAQAGAKAM
     TAFQPDVIIA LGGGSAMDAG KIMWVMYEHP EVDFKDMAMR FIDIRKRVYT FPKMGEKAYF
     VAIPTSSGTG SEVTSFAVIT DQETGVKYPL ADYELMPKMA IIDADNMMSQ PKGLTSASGV
     DVLVHSLEAY VSVMASDYTD GLALKAMKNV FDYLPIAYND GSNVEARCKM ADASCMAGMA
     FNNAFLGVCH SMAHKLGAFH HLPHGIANAL LLNLVIEFNS AECPRKMGTF SQYEYPHTMA
     KYAECARFCG VQAKTDEEAV QKFLVKISEL KEAVGVKKTI KEYGVDEKYF LDTLDAMVEQ
     AFDDQCTGAN PRYPLMSEIK EMYLKAYYGK
//