ID K2LW95_TRYCR Unreviewed; 351 AA.
AC K2LW95;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=NADP-dependent alcohol hydrogenase, putative {ECO:0000313|EMBL:EKF26983.1};
GN ORFNames=MOQ_009306 {ECO:0000313|EMBL:EKF26983.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF26983.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF26983.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF26983.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
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:EKF26983.1}.
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DR EMBL; AHKC01019546; EKF26983.1; -; Genomic_DNA.
DR AlphaFoldDB; K2LW95; -.
DR EnsemblProtists; EKF26983; EKF26983; MOQ_009306.
DR OrthoDB; 1550at2759; -.
DR Proteomes; UP000007350; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 351 AA; 37433 MW; 2D3074B9801749A7 CRC64;
MATNAKGYAA PSAKAPLAPF SFQRRAVGAD DVSIKILFCG VCHSDIHQAR DEWGGSLFPM
VPGHEIVGQV TSVGANVKKF KVGDTAGVGC MVDSCEKCVE CKKGLEQFCV EGSTSTYGSR
ARGSNEPTYG GYSDHIVVKE SFVLRIPSNL NLAATAPLLC AGITTYSPLR HWGTKAGTKV
GVVGLGGLGH MAVKIAKAMG AEVTVFTTSE SKREAARLLG ADHVIISKDP EQMKAVKNTL
NLIIDTVGNT HDLSPYINAL TTDGVHVLVG LPENPNPPVS SYLLIRGRKS ISGSLIGGIP
ETQEMLDFCG KHNIVSDIEL ISMDYINTAY ERVTKSDVRY RFVIDMATIG Q
//
