ID A0A077LQ82_9PSED Unreviewed; 340 AA.
AC A0A077LQ82;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=NADPH:quinone reductase {ECO:0000313|EMBL:BAP46267.1};
GN ORFNames=PSCI_5565 {ECO:0000313|EMBL:BAP46267.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP46267.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP46267.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP46267.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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; AP014637; BAP46267.1; -; Genomic_DNA.
DR RefSeq; WP_045493517.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077LQ82; -.
DR STRING; 1028989.PSCI_5565; -.
DR KEGG; pses:PSCI_5565; -.
DR HOGENOM; CLU_026673_11_2_6; -.
DR OrthoDB; 9785812at2; -.
DR Proteomes; UP000031652; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08259; Zn_ADH5; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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 InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR48106:SF8; QUINONE OXIDOREDUCTASE PIG3; 1.
DR PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031652};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..337
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 340 AA; 35654 MW; E9ACAA2B7080BD77 CRC64;
MKAIVLKGFG GPEQLQVEEV PTPQPGRGEV LVRVHAAGVC HHDLLHRAGQ LPGAHTGVVL
GHEVAGEVVQ VGDDVLNLAV GARVVIYQRR FCGQCRQCLR GRQDLCRALG LPSVDTEGAY
AEYLRVPAIS AVPLPEGLDY VQAALASCPI ATSVRALHGE AALKPGETVL INGASGGLGA
HQIQLARALG ARVIAVTGSA EKREFLEALG AHEVIVSNGS YSAEVWRLTG KRGVDVAIEN
LGHMLEDTLR SMSLGGRVVV LGNVSPGAVA VNPGLLIGRR LKLQGSGSAT LEELRTALAL
IAAGQVRPLI DRVLPFPEVA QAHALLESRQ VNGRIVLSGW
//
