ID A0A1H9TIP3_9SPHI Unreviewed; 385 AA.
AC A0A1H9TIP3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SER97031.1};
GN ORFNames=SAMN04488023_12317 {ECO:0000313|EMBL:SER97031.1};
OS Pedobacter rhizosphaerae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=390241 {ECO:0000313|EMBL:SER97031.1, ECO:0000313|Proteomes:UP000199572};
RN [1] {ECO:0000313|EMBL:SER97031.1, ECO:0000313|Proteomes:UP000199572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18610 {ECO:0000313|EMBL:SER97031.1,
RC ECO:0000313|Proteomes:UP000199572};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOGG01000023; SER97031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9TIP3; -.
DR STRING; 390241.SAMN04488023_12317; -.
DR OrthoDB; 9787435at2; -.
DR Proteomes; UP000199572; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 InterPro; IPR020843; PKS_ER.
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 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199572};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..383
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 385 AA; 41909 MW; 5660C68BA7AA285C CRC64;
MKAAVFHKPG DIRVDTVPDP KILDPRDIIL KVTSTAICGS DLHILSGAVP QKDPMVMGHE
FMGIVEEVGS AITNLKVGDR VVVPFPISCG KCFFCTHEAS PACEDSNYKN YGPAGNVADQ
KGGALFGYTD LYGGYSGGQA QYVRVPYADI SPRVVPEHLS DEQALFLTDI FPTGWSAIDW
AQLKGGETVA IFGSGPVGLM AQKAAWINGA ARVIAIDPLD YRLERARTAN NVETLNPHKV
DVVEAIREMT GGRGADVCVD AVGFEPERSL IDKLKATIHF EKGSMKVLEM CFESVRRMGT
VSIMGVYGSP YDNFPLFRMF DKGITIKQGQ APVLNYIDKL IALVSEGKVV LDDIITHTLP
LEDAAHAYKI FDEKQEDCVK VVLKP
//