ID A0A3S1BN59_9BACT Unreviewed; 366 AA.
AC A0A3S1BN59;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NAD(P)-dependent alcohol dehydrogenase {ECO:0000313|EMBL:NSL87021.1};
GN ORFNames=ECE50_009280 {ECO:0000313|EMBL:NSL87021.1};
OS Chitinophaga solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1233460 {ECO:0000313|EMBL:NSL87021.1, ECO:0000313|Proteomes:UP000281028};
RN [1] {ECO:0000313|EMBL:NSL87021.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mgbs1 {ECO:0000313|EMBL:NSL87021.1};
RA Goh C.B.S., Lee M.S., Parimannan S., Pasbakhsh P., Yule C.M., Rajandas H.,
RA Loke S., Croft L., Tan J.B.L.;
RT "Chitinophaga laudate sp. nov., isolated from a tropical peat swamp.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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:NSL87021.1}.
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DR EMBL; RIAR02000001; NSL87021.1; -; Genomic_DNA.
DR Proteomes; UP000281028; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 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 InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 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|RuleBase:RU361277};
KW Reference proteome {ECO:0000313|Proteomes:UP000281028};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
SQ SEQUENCE 366 AA; 38959 MW; B0F7967326E96203 CRC64;
MDIKAAIFKQ PKQPFEFEHV QLDELKEGEV LVKLVATGVC HTDISVWEAN FPFGYPGILG
HEGAGIVEAV GPGVTKVKAG NHVLLHIAAC GKCEYCISGT PAYCKDMLPL NFSGRRPDGS
CPYHLHGEDL NGLFFYQSSF ATYSIASERN VVAIPDDLPL PVMAPLGCGF ITGAGTVMNT
LKAEPGTSIA IFGAGSVGLA AVMAAKIAGC TTIVTIDIND ERLALAKELG ATHTINGRNS
NSSEEIQTRI IPGGVNFSID TTGDSSVIQH AVTALRILGT CALVAVRTVG AKQEFDYLNL
ALGRTVKGVI AGDSIPEIFI PRLISFYRQG LFPIDRLISF YNFEDINNAI QDAGSGKTIK
AVLLMQ
//
