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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//