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Database: UniProt
Entry: A0A011UFZ4_RUMAL
LinkDB: A0A011UFZ4_RUMAL
Original site: A0A011UFZ4_RUMAL 
ID   A0A011UFZ4_RUMAL        Unreviewed;       905 AA.
AC   A0A011UFZ4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=RASY3_06725 {ECO:0000313|EMBL:EXM39559.1};
OS   Ruminococcus albus SY3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM39559.1, ECO:0000313|Proteomes:UP000021369};
RN   [1] {ECO:0000313|EMBL:EXM39559.1, ECO:0000313|Proteomes:UP000021369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY3 {ECO:0000313|EMBL:EXM39559.1,
RC   ECO:0000313|Proteomes:UP000021369};
RA   Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA   Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six Ruminococcal strains.";
RL   Submitted (JUN-2013) 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:EXM39559.1}.
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DR   EMBL; JEOB01000002; EXM39559.1; -; Genomic_DNA.
DR   RefSeq; WP_037286291.1; NZ_JEOB01000002.1.
DR   AlphaFoldDB; A0A011UFZ4; -.
DR   PATRIC; fig|1341156.4.peg.1763; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000021369; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021369}.
FT   DOMAIN          13..314
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          461..852
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   905 AA;  98148 MW;  1084687BC2941ACA CRC64;
     MAKKEYEIVD GVEKLEAALE RVRAAQRKMA TFTQEQVDRI FLAAATAANR ARIDLAEQAV
     AETGMGIVED KVIKNHYASE YIYNKYRDTK TCGVLEEDKS AGIKKIAEPI GVIGAVIPTT
     NPTSTAIFKS LIALKTRNGI IISPHPRAKE STIAAAKVVL EAAVEAGAPE DIIAWIDIPS
     LEMTNMLMKE VDIILATGGP GMVHAAYSSG KPALGVGAGN TPAIIDDSAD ILLAVNSIIH
     SKTFDNGMIC ASEQSVIVLD SIYDAVKTEF AARGCYFLKP DELNKVRKTI IINGALNAKI
     VGQSAAKIAE LAGVTVPEGS KILIGEVESV DISEEFAHEK LSPVLAMYKA SDIQDAFGKA
     EHLIADGGYG HTASIYLDAV REQEKLSEFG ERMKTCRILV NTPSSQGGIG DLYNFKLAPS
     LTLGCGSWGG NSVSENVGVK HLLNIKTVAE RRENMLWFRA PEKVYFKKGC LPVALDELKN
     VMGKKKAFIV TDSFLFKNGF TKPVTDKLDE MGIVHETFSD VAPDPTLACA VEGVKAIRSF
     EPDVIIAIGG GSAMDAAKIM WVMYEHPEAD FMDMAMRFVD IRKRIYTFPK MGEKAYFICV
     PTSSGTGSEV TPFAVITDDK TGHKYPLADY ELMPNMAIVD TDMMMSAPKG LTAASGLDCM
     VHDLEALVSV MATPFTDGIA LESLKMTFDN LPECVENGQT AVRARENMAH AATMAGMAFA
     NAFLGIGHSL AHKLGAYHHL PHGICCALVI SEVIRFNASD VPVKMGTFPQ YEYPQAAAKY
     ARIARYLGVQ GSGDNELVEG LIAKIEELKE AVGCKKTIAE YGISEEDFLA TLDKMSRDAF
     DDQCTGANPR YPLISELKQI YMNVYYGRTF TETEKPDASQ IDSAESSKDF KQAFNRAVSS
     GKKRV
//
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