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Database: UniProt
Entry: I3VSF1_THESW
LinkDB: I3VSF1_THESW
Original site: I3VSF1_THESW 
ID   I3VSF1_THESW            Unreviewed;       859 AA.
AC   I3VSF1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   OrderedLocusNames=Tsac_0416 {ECO:0000313|EMBL:AFK85446.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK85446.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK85446.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
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; CP003184; AFK85446.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3VSF1; -.
DR   SMR; I3VSF1; -.
DR   STRING; 1094508.Tsac_0416; -.
DR   KEGG; tsh:Tsac_0416; -.
DR   PATRIC; fig|1094508.3.peg.421; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   BioCyc; TSAC1094508:GLMA-415-MONOMER; -.
DR   BRENDA; 1.1.1.1; 6289.
DR   BRENDA; 1.1.1.27; 6289.
DR   BRENDA; 1.2.1.10; 6289.
DR   Proteomes; UP000006178; Chromosome.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
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; IPR039697; Alcohol_dehydrogenase_Fe.
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; IPR012079; Bifunc_Ald-ADH.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 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; PS00913; ADH_IRON_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111}.
FT   DOMAIN          10..405
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          460..847
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   COILED          783..830
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   859 AA;  94804 MW;  3CD0DD8A870D1710 CRC64;
     MATTKTELDV QKQIDLLVSR AQEAQKKFMS YTQEQIDAIV KAMALAGVDK HVELAKMAYE
     ETKMGVYEDK ITKNLFATEY VYHDIKNEKT VGIINENIEE NYMEVAEPIG VIAGVTPVTN
     PTSTTMFKCL ISIKTRNPII FSFHPKAIKC SIAAAKVMYE AALKAGAPEG CIGWIETPSI
     EATQLLMTHP GVSLILATGG AGMVKAAYSS GKPALGVGPG NVPCYIEKSA NIKRAVSDLI
     LSKTFDNGVI CASEQAVIID EEIADEVKKL MKEYGCYFLN KDEIKKLEKF AIDEQSCAMS
     PAVVGQPAAK IAEMAGFKVP EGTKILVAEY EGVGPKYPLS REKLSPILAC YTVKDYNEGI
     KKCEEMTEFG GLGHSAVIHS ENQNVINEFA RRVRTGRLIV NSPSSQGAIG DIYNTNTPSL
     TLGCGSMGRN STTDNVSVKN LLNIKRVVIR KDRMKWFKIP PKIYFESGSL QYLCKVKRKK
     AFIVTDPFMV KLGFVDKVTY QLDKANIEYE IFSEVEPDPS VDTVMNGVKI MNSYNPDLII
     AVGGGSAIDA AKGMWLFYEY PDTEFETLRL KFADIRKRAF KFPELGKKAL FIAIPTTSGT
     GSEVTAFAVI TDKKRNIKYP LADYELTPDI AIIDPDLTKT VPPSVTADTG MDVLTHAIEA
     YVSVMASDYT DALAEKAIKI VFEYLPRAYK NGNDEEAREK MHNASCMAGM AFTNAFLGIN
     HSMAHILGGK FHIPHGRANA ILLPYVIRYN AEKPTKFVAF PQYEYPKAAE RYAEIAKFLG
     LPASTVEEGV ESLIEAIKNL MKELNIPLTL KDAGINKEQF EKEIEEMSDI AFNDQCTGTN
     PRMPLTKEIA EIYRKAYGA
//
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