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
//