ID   A0A1G6CYN1_9FIRM        Unreviewed;       869 AA.
AC   A0A1G6CYN1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=SAMN02910317_01873 {ECO:0000313|EMBL:SDB38023.1};
OS   Ruminococcaceae bacterium FB2012.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB38023.1, ECO:0000313|Proteomes:UP000199364};
RN   [1] {ECO:0000313|EMBL:SDB38023.1, ECO:0000313|Proteomes:UP000199364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB2012 {ECO:0000313|EMBL:SDB38023.1,
RC   ECO:0000313|Proteomes:UP000199364};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMXS01000009; SDB38023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6CYN1; -.
DR   STRING; 1520817.SAMN02910317_01873; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000199364; 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; 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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199364}.
FT   DOMAIN          14..405
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          462..856
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   COILED          6..36
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   869 AA;  94993 MW;  FED225FD02843418 CRC64;
     MADFKATSLV DSVEALEEKL RQVKEAQRIY STYSQEQVDK IFKAAAIAAN MARVPLAKMA
     VEETGMGVIE DKVIKNNFAA EYIYNKYKDT QTCGIIEENK SMGTKKVLEP IGVVAAVIPT
     TNPTSTAIFK TMLCLKTRNG IIISPHPRAK KSTIEAARIV YEAAVKAGAP EHIIGWIDVP
     SLEMTNLVMK EADIILATGG PGMVKSAYSS GKPAIGVGAG NTPAVIDETA DIKLAVNSII
     HSKTFDNGMI CASEQSVIIE KSIYDAAKAE FIARGCHVCT PEECDKVRHT IIINGALNAK
     IVGQSAYKIA QLAGFEVPKS TKILIGEVER VDIDEEFAHE KLSPVLAMYK ADSFEDAMEK
     ADRLIQDGGF GHTSSLYVDA VTQTDKINRF AEKMKTCRIL VNTPSSHGGI GDLYNFNLTP
     SLTLGCGSWG GNSVSENVGV KHLLNVKTVA ERRENMLWFR APEKVYFKRG CLPIALEELK
     AVMGKKRAFI VTDSFLFKNG FTRPVTDKLD ELGIVHETFS DVAPDPTLAC ALEGVKMLRN
     FEPDTIIAIG GGSAMDAAKI MWVLYEHPEA DFYDMAMRFI DIRKRVYTFP KMGEKAYMVC
     VPTSSGTGSE VTPFAVISDD QTGHKYPLAD YELMPNMAII DADLMMSAPK GLTAASGLDC
     MVHDLEALAS VMATDFTDGI ALQSLKQTFD NLPECVEHGQ TAYRARENMA HAATMAGMAF
     ANAFLGIGHS LAHKLGAYHH LPHGICCALV ITEVMKFNAD PAPAKMGTFP QYEYPNTLAK
     YAQTARYLGI TGKDDQECFD KLCDKVEELK SAVGCKKTIA DYGISEEDFL ATLDQMSEDA
     FDDQCTGANP RYPLIEELKE IYTKCYYGK
//