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Database: UniProt
Entry: E3D2G4_NEIM7
LinkDB: E3D2G4_NEIM7
Original site: E3D2G4_NEIM7 
ID   E3D2G4_NEIM7            Unreviewed;       354 AA.
AC   E3D2G4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Zinc-binding alcohol dehydrogenase {ECO:0000313|EMBL:ADO31110.1};
DE            EC=1.1.1.4 {ECO:0000313|EMBL:ADO31110.1};
GN   OrderedLocusNames=NMBB_0667 {ECO:0000313|EMBL:ADO31110.1};
OS   Neisseria meningitidis serogroup B (strain alpha710).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO31110.1, ECO:0000313|Proteomes:UP000006929};
RN   [1] {ECO:0000313|EMBL:ADO31110.1, ECO:0000313|Proteomes:UP000006929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alpha710 {ECO:0000313|Proteomes:UP000006929};
RX   PubMed=20709895; DOI=10.1128/JB.00883-10;
RA   Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H.,
RA   Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.;
RT   "Comparative genome biology of a serogroup B carriage and disease strain
RT   supports a polygenic nature of meningococcal virulence.";
RL   J. Bacteriol. 192:5363-5377(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; CP001561; ADO31110.1; -; Genomic_DNA.
DR   RefSeq; WP_002214294.1; NC_017505.1.
DR   AlphaFoldDB; E3D2G4; -.
DR   KEGG; nmp:NMBB_0667; -.
DR   PATRIC; fig|630588.3.peg.800; -.
DR   HOGENOM; CLU_026673_11_0_4; -.
DR   OMA; FILGHEC; -.
DR   Proteomes; UP000006929; Chromosome.
DR   GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08233; butanediol_DH_like; 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; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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   ECO:0000313|EMBL:ADO31110.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..350
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   354 AA;  37908 MW;  CEEEA6CFE0C57B90 CRC64;
     MKAARFYDKG DIRIEDIPEP TVAPGTVGIN VAWCGICGTD LHEFMEGPIF IPPCGHPHPI
     SGESAPVTMG HEFSGVVYAV GEGVDDIKVG QHVVVEPYII RDDVPTGEGS NYHLSKDMNF
     IGLGGCGGGL SEKIAVKRRW VHPISDKIPL DQAALIEPLS VGHHAYVRSG AKAGDVALVG
     GAGPIGLLLA AVLKAKGIKV IITELSKARK DKARESGVAD YILDPSEVDV VEEVKKLTNG
     EGVDVAFECT SVNKVLDTLV EACKPAANLV IVSIWSHPAT VNVHSVVMKE LDVRGTIAYC
     NDHAETIKLV EEGKINLEPF ITQRIKLDEL VSEGFERLIH NNESAVKIIV SPNL
//
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