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Database: UniProt
Entry: A0A099TWC4_9HELI
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Original site: A0A099TWC4_9HELI 
ID   A0A099TWC4_9HELI        Unreviewed;       365 AA.
AC   A0A099TWC4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=NAD(P)-dependent alcohol dehydrogenase {ECO:0000313|EMBL:TLE00181.1};
DE   SubName: Full=NADP-dependent alcohol dehydrogenase {ECO:0000313|EMBL:STQ87008.1};
DE            EC=1.1.1.2 {ECO:0000313|EMBL:STQ87008.1};
GN   Name=cad {ECO:0000313|EMBL:STQ87008.1};
GN   ORFNames=LS73_005725 {ECO:0000313|EMBL:TLE00181.1}, NCTC12714_01819
GN   {ECO:0000313|EMBL:STQ87008.1};
OS   Helicobacter muridarum.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=216 {ECO:0000313|EMBL:STQ87008.1, ECO:0000313|Proteomes:UP000255139};
RN   [1] {ECO:0000313|EMBL:TLE00181.1, ECO:0000313|Proteomes:UP000029922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST1 {ECO:0000313|EMBL:TLE00181.1,
RC   ECO:0000313|Proteomes:UP000029922};
RX   PubMed=25428971;
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Draft genome sequences of eight enterohepatic helicobacter species
RT   isolated from both laboratory and wild rodents.";
RL   Genome Announc. 2:e01218-e01214(2014).
RN   [2] {ECO:0000313|EMBL:STQ87008.1, ECO:0000313|Proteomes:UP000255139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ87008.1,
RC   ECO:0000313|Proteomes:UP000255139};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; UGJE01000002; STQ87008.1; -; Genomic_DNA.
DR   EMBL; JRPD02000010; TLE00181.1; -; Genomic_DNA.
DR   RefSeq; WP_034558626.1; NZ_UGJE01000002.1.
DR   AlphaFoldDB; A0A099TWC4; -.
DR   STRING; 216.LS73_07435; -.
DR   OrthoDB; 5295340at2; -.
DR   Proteomes; UP000029922; Unassembled WGS sequence.
DR   Proteomes; UP000255139; Unassembled WGS sequence.
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; DEATH RESISTOR ADH DOMAIN CONTAINING TARGET, ISOFORM C; 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:STQ87008.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255139};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..356
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   365 AA;  40069 MW;  7C89EB22C8F08193 CRC64;
     MLLKENLIQA QNGQRITAKG YAVAHKSDTF KPFSFSRHAL GENDILIEIL FAGICHSDIH
     SAREEWHKGI FPMVPGHEIA GRVVAVGSNV NKFKVGDYAG VGCMVNSCGE CEACKRSQEQ
     FCENGKCVFT YDCRDCFHDN EPTYGGYSNN IVVSEKFAVN FPQDAPLEKV APLLCAGITT
     YSPIKFSKVK AGDKVAVAGF GGLGVMALKY AIKMGAEVSV FARNKNKEKE ALELGAKTLY
     TDTKGVKERF DFIISTIPTA YDINAYAELL KFGGEMAIVG LPPASENLKI DLTRLVFAAG
     KKVYGSLIGG MKETQEMLDF SLKHKIYPET EVISVEQINE AYENLISGKA KFRYVIDMSS
     IKGQE
//
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