ID A0A162TE25_9CLOT Unreviewed; 378 AA.
AC A0A162TE25;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KZL92527.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:KZL92527.1};
DE EC=1.1.1.4 {ECO:0000313|EMBL:KZL92527.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:KZL92527.1};
GN Name=adh {ECO:0000313|EMBL:KZL92527.1};
GN ORFNames=CLMAG_23410 {ECO:0000313|EMBL:KZL92527.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL92527.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL92527.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL92527.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KZL92527.1}.
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DR EMBL; LWAE01000002; KZL92527.1; -; Genomic_DNA.
DR RefSeq; WP_066622063.1; NZ_LWAE01000002.1.
DR AlphaFoldDB; A0A162TE25; -.
DR STRING; 1121326.CLMAG_23410; -.
DR PATRIC; fig|1121326.3.peg.2338; -.
DR OrthoDB; 9769198at2; -.
DR Proteomes; UP000076603; Unassembled WGS sequence.
DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KZL92527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..141
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 189..256
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 378 AA; 41597 MW; 9E30BA2204BF0B3C CRC64;
MKAVTFQGIK NVKVKDVQAP KIQKSDDIIV KLTSTAICGS DLHLIHDMVP NIHQDYIIGH
EPMGIVEEVG PEVTKVKKGD RVIVPFNVSC GECFFCKHDL TCMCDNSNPN GENGGFFGYS
ETFGGYPGGQ AEFMRVPYGN FTPFRIPDDC EVEDEKLLLM SDAMATAYWS VENAGVKKGN
TVIILGCGPI GLLAQKFAWL HGAERVIAVD YIDYRLEHAK KHNKVEIVNF EQHQNTGEYL
REITHGGADI VIDCVGMDGK MTPLEFLGSG VKLQSGALGA FIMATQAVRK GGMIQVTGVY
GGRYNAFPFG DIMNRNINIR TGQAPVIPYM PKLYSLLTEG KVDPSDIITH RLPLDKAEYG
YEVFDTKTDG CIKVVLKT
//
