ID A0A1M6KAL7_9FIRM Unreviewed; 432 AA.
AC A0A1M6KAL7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Alcohol dehydrogenase, class IV {ECO:0000313|EMBL:SHJ55966.1};
GN ORFNames=SAMN02745751_02845 {ECO:0000313|EMBL:SHJ55966.1};
OS Dethiosulfatibacter aminovorans DSM 17477.
OC Bacteria; Bacillota; Tissierellia; Dethiosulfatibacter.
OX NCBI_TaxID=1121476 {ECO:0000313|EMBL:SHJ55966.1, ECO:0000313|Proteomes:UP000184052};
RN [1] {ECO:0000313|EMBL:SHJ55966.1, ECO:0000313|Proteomes:UP000184052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17477 {ECO:0000313|EMBL:SHJ55966.1,
RC ECO:0000313|Proteomes:UP000184052};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; FQZL01000025; SHJ55966.1; -; Genomic_DNA.
DR RefSeq; WP_073050233.1; NZ_FQZL01000025.1.
DR AlphaFoldDB; A0A1M6KAL7; -.
DR STRING; 1121476.SAMN02745751_02845; -.
DR OrthoDB; 9801156at2; -.
DR Proteomes; UP000184052; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08189; Fe-ADH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000184052}.
FT DOMAIN 27..373
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT REGION 400..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 48724 MW; D89A7D3AA399DACE CRC64;
MNKLMIRTRH TIRKQTRRSS RYPEPVVVIE SGCSSQVAAY LKKHNSEKTL VVTDKKIIKL
KIMDEFVSSL RNEGIDYIVF NNIVENPTID NVVEGVEVYR TNHCDSIIGF GGRAAMDGAK
LIGAKVTNKK DVYSMKGRNR LWRRPPMFIA VPTIAGTGSE ADFKAIVTDT NRFEKITVID
KKLLPEISYL DANLMKEVPT QILACSGMNL LAKTMESYLS RYRTKAAEKL CIETVQIVFN
NLEKLYDDRM DSDAGSSLFT ASYFSGRANM VALTGYGDLI GYFLSDAYGI SHSYVLAVVF
PYLLEMSRDK IIKRLSRLAV LVGLGDENED ASVLSDRIIS RIKEMNANMG IPEYIEVLRE
RDIKVIAGII EKNSNPKVPA PKILDAEDFE KLLYSVLKKD EGNKEEDETS ELKEDIISYN
EVEETNDTEN EL
//