ID Q82WE2_NITEU Unreviewed; 371 AA.
AC Q82WE2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=Zinc-containing alcohol dehydrogenase superfamily {ECO:0000313|EMBL:CAD84653.1};
DE EC=1.1.1.90 {ECO:0000313|EMBL:CAD84653.1};
GN OrderedLocusNames=NE0742 {ECO:0000313|EMBL:CAD84653.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD84653.1, ECO:0000313|Proteomes:UP000001416};
RN [1] {ECO:0000313|EMBL:CAD84653.1, ECO:0000313|Proteomes:UP000001416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC {ECO:0000313|Proteomes:UP000001416};
RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA Whittaker M., Arp D.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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; AL954747; CAD84653.1; -; Genomic_DNA.
DR RefSeq; WP_011111360.1; NC_004757.1.
DR AlphaFoldDB; Q82WE2; -.
DR STRING; 228410.NE0742; -.
DR KEGG; neu:NE0742; -.
DR eggNOG; COG1062; Bacteria.
DR HOGENOM; CLU_026673_14_1_4; -.
DR OrthoDB; 9770544at2; -.
DR PhylomeDB; Q82WE2; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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:CAD84653.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..367
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 371 AA; 39517 MW; C442949CA58A6194 CRC64;
MRRIRAAVVY QKGGPFQIED LRLEAPRTDE VLVRIVATGM CHTDMVARDQ LYDVPLPVVL
GHEGSGIVEQ IGDGVRKVAV GNHVVLTYMW CGHCKPCLRG DLTYCEHFYA LNFGGVREDG
STSTCLANDT RRPIHDHFFG QSSFGTFALV HERNVIKVPE TAPLELLGPL GCGIQTGAGA
VINTLKVSPG SSFVAFGGGA VGLSAVMAAH AAGATTIISV DVVPSRLALA MELGATHTIN
SRETDPVEAV HKIINGGADF TLESSGRPAV LRQAIDALAI RGTCGIVGAP ALGTEASFDV
NGVMTTGKRI IGIVEGDSKP DLFIPALVEL YQQGKFPFDR LVKFYSLDQI NQAAEDSEKG
ITIKPIIRLQ S
//
