ID E3D3Y1_NEIM7 Unreviewed; 339 AA.
AC E3D3Y1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN OrderedLocusNames=NMBB_2379 {ECO:0000313|EMBL:ADO32490.1};
OS Neisseria meningitidis serogroup B (strain alpha710).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO32490.1, ECO:0000313|Proteomes:UP000006929};
RN [1] {ECO:0000313|EMBL:ADO32490.1, 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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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DR EMBL; CP001561; ADO32490.1; -; Genomic_DNA.
DR RefSeq; WP_014575617.1; NC_017505.1.
DR AlphaFoldDB; E3D3Y1; -.
DR KEGG; nmp:NMBB_2379; -.
DR PATRIC; fig|630588.3.peg.2773; -.
DR HOGENOM; CLU_026673_3_0_4; -.
DR Proteomes; UP000006929; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000,
KW ECO:0000313|EMBL:ADO32490.1}; Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 13..334
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 36609 MW; A1292BFB381F4A6D CRC64;
MKAIGFTRPL PVSNPEALLD INLPEPELRP HDILVAVQAV SVNPVDVKVR AAHTSEGGAY
RVLGYDAAGI VQAVGSEVRN FQVGDEVYYA GALNRQGSNA QLQAVDARIA AKKPRSLDFA
QAAALPLTAI TAWETLFDRL DVNKPVAGDA NALLLIGGAG GVGSLAIQFL KKLTDIQVIA
TASRPESRSW VEKLGADFVI NHHENMAEQI AALNIGAPSF VFSTNHTDRH LPQIVELIAP
QGRIALIDDP ETLDVNPLKG KSLSLHWEFM FTRPLSETAD IERQGEILAE TARLVDEGII
RPTATQILHG INAANLRRAH EMLESGDMIG KLVLEGWDN
//
