ID D6YUS4_WADCW Unreviewed; 360 AA.
AC D6YUS4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=NADP-dependent alcohol dehydrogenase C {ECO:0000313|EMBL:ADI37885.1};
DE EC=1.1.1.2 {ECO:0000313|EMBL:ADI37885.1};
GN Name=adhC {ECO:0000313|EMBL:ADI37885.1};
GN OrderedLocusNames=wcw_0514 {ECO:0000313|EMBL:ADI37885.1};
OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI37885.1, ECO:0000313|Proteomes:UP000001505};
RN [1] {ECO:0000313|EMBL:ADI37885.1, ECO:0000313|Proteomes:UP000001505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT "The Waddlia genome: a window into chlamydial biology.";
RL PLoS ONE 5:E10890-E10890(2010).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP001928; ADI37885.1; -; Genomic_DNA.
DR AlphaFoldDB; D6YUS4; -.
DR STRING; 716544.wcw_0514; -.
DR KEGG; wch:wcw_0514; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_0; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000001505; Chromosome.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADI37885.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001505};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..353
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 360 AA; 39347 MW; A4ACE0BFC4B535CB CRC64;
MLKDKKKEAP VSKTVKAYAA PTAEKPLSQT TINRRSPTSK DVVIDIHYCG VCHSDLHTAR
NEWQNTTYPC VPGHEIVGIV VETGSGATKY QKGDKVAVGC LVDSCRTCSS CKENLEQHCE
NGATMTYNSP DKHLKDTTYG GYSEMIVVDE DFVLKMPDNL DFAAAAPLLC AGITTYSPLR
QYNVGPGQKV GVVGLGGLGH MGVKLAAAMG AEVTVLTHSD NKREDALKLG AKDVIYTKDQ
NQLEKAVNRF DFILDTVSAE HDLNLYLNLL KCSGAMVLVG APPEPVPVAA FSLIFQRRKL
AGSLIGGLKE TQEMLDFCGK HNIVCDVEMI HIDQINEAYE RMLKSDVKYR FVIDMKSLKG
//
