ID A0A1M6ZZX5_PSETH Unreviewed; 344 AA.
AC A0A1M6ZZX5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase {ECO:0000313|EMBL:SHL35960.1};
GN ORFNames=SAMN05443637_12585 {ECO:0000313|EMBL:SHL35960.1};
OS Pseudonocardia thermophila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1848 {ECO:0000313|EMBL:SHL35960.1, ECO:0000313|Proteomes:UP000184363};
RN [1] {ECO:0000313|EMBL:SHL35960.1, ECO:0000313|Proteomes:UP000184363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43832 {ECO:0000313|EMBL:SHL35960.1,
RC ECO:0000313|Proteomes:UP000184363};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRAP01000025; SHL35960.1; -; Genomic_DNA.
DR RefSeq; WP_073460046.1; NZ_FRAP01000025.1.
DR AlphaFoldDB; A0A1M6ZZX5; -.
DR STRING; 1848.SAMN05443637_12585; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000184363; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:UP000184363};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 344 AA; 35358 MW; F83E6059F3C8B561 CRC64;
MKAVLYAGDG EVRVDSVAEP DVLAPTDAVV RVRRAAVCGT DLHLVAHDAG LPRGTVLGHE
FAGEVVAVGD AVHGHALGDL VAGADFTACG QCWWCRRGDH WECADRRFFG TGVTYGPALA
GAQAELVRVP FADTVLRPVP DGVPLDAAVL LGDTLATGYA AIRRAELAPG DSTVVVGGGP
VGQLTSLVAQ ACGAGAVVVV EPVAPRRALA AAEGALVTDP DGAAELVAAI TDGRGADVVV
DAIGGAAGLD TAFTLVRKRG TIVSVGVPTM QTHSVPVQRA FADELTLRFA IGDVMRDGDQ
ITALVRSGAV DPTVIVTETV PLDEVPQAYR RMAERRTLKS LVTV
//