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Database: UniProt
Entry: A0A1Y3YEL3_9FIRM
LinkDB: A0A1Y3YEL3_9FIRM
Original site: A0A1Y3YEL3_9FIRM 
ID   A0A1Y3YEL3_9FIRM        Unreviewed;       872 AA.
AC   A0A1Y3YEL3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=B5G00_05220 {ECO:0000313|EMBL:OUN93769.1};
OS   Blautia sp. An46.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1965636 {ECO:0000313|EMBL:OUN93769.1, ECO:0000313|Proteomes:UP000196301};
RN   [1] {ECO:0000313|Proteomes:UP000196301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An46 {ECO:0000313|Proteomes:UP000196301};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUN93769.1}.
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DR   EMBL; NFIF01000004; OUN93769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3YEL3; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000196301; 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:UP000196301}.
FT   DOMAIN          16..277
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          465..857
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   872 AA;  95296 MW;  05E817413DD8A626 CRC64;
     MAKKTESNVP ETVNSVEALQ AKIASMREAQ KKFASYSQEQ VDKIFFEAAM AANKQRIPLA
     RMACEETGMG VLEDKVIKNH YAAEYTYNAY KRVKTCGVVE EDKSYGIKKI AEPVGIVGAV
     IPTTNPTSTA IFKCLICLKT RNAIIISPHP RAKKCTIEAA KVVLEAAVKA GAPEGIIGWV
     EEPTLELSNE LMRSADVILA TGGPGMVKAA YSSGKPAIGV GPGNVPVIMD STCDIQTAVY
     SVIHSKTFDN GMICASEQSV TAIADIYDKV KAEFVKRGCH VLNSEELDKV RKIILTEAGT
     VNARIVGQPA SVIAELAGIS VPKDTKILIG EVTSVDISDP FAHEKLSPVL ALYKAKDFDT
     ALDMADQLVK DGGYGHTASI YVHPSQTEKL DKFADRMKTC RILVNTPSSH GGIGDLYNFK
     LAPSLTLGCG SYGGNSVSEN VGVKHLLNTK TVAERRENML WFRTPEKVYF KKGCLPVALD
     ELRTVYGKKK AFIVTDTFLY QSGYTKPITD KLDEMGIQYD CFFDVAPDPT LQCAQKGLEQ
     LKDFGPDTII ALGGGSAMDA AKIMWLMYEH PECKFEDLAM DFMDIRKRVY VFPKMGIKAM
     MVAIPTSSGT GSEVTPFAII TDATTGTKWP IADYELMPNM AIVDTDFMMT QPKGLTSASG
     IDALTHALEA YASIMATDFT DGMALKAAKL IFDYLPSAYE KGAADPIARE KMANASTLAG
     MAFSNAFLGI CHSMAHKLGA YHHLPHGIAN ALLIEHVMRY NADPAPTKMG TFSQYPYPHA
     KERYCEMARF VGIQGKDDDE VFENFIKAIA DLKAKVGIKR TIKEYGITEE DFMATLDEMV
     ENAFNDQCTG ANPRYPLMSE MKEMYLKAYH EG
//
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