ID A0A0Q4SCI4_9FLAO Unreviewed; 347 AA.
AC A0A0Q4SCI4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=NADPH-quinone reductase {ECO:0000313|EMBL:KQO28656.1};
GN ORFNames=ASF10_22805 {ECO:0000313|EMBL:KQO28656.1};
OS Flavobacterium sp. Leaf82.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736238 {ECO:0000313|EMBL:KQO28656.1, ECO:0000313|Proteomes:UP000051828};
RN [1] {ECO:0000313|EMBL:KQO28656.1, ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|EMBL:KQO28656.1,
RC ECO:0000313|Proteomes:UP000051828};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|Proteomes:UP000051828};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|Proteomes:UP000051828};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQO28656.1}.
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DR EMBL; LMMA01000014; KQO28656.1; -; Genomic_DNA.
DR RefSeq; WP_056249179.1; NZ_LMMA01000014.1.
DR AlphaFoldDB; A0A0Q4SCI4; -.
DR OrthoDB; 9787435at2; -.
DR Proteomes; UP000051828; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05289; MDR_like_2; 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; 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; PTHR44013; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C16A3.02C; 1.
DR PANTHER; PTHR44013:SF1; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C16A3.02C; 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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
FT DOMAIN 26..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 347 AA; 37274 MW; 3EED74890CCC8865 CRC64;
MTSLEKKANP IETPSKMMAI RLHEFGGTEV LRYEEAPVPK LKSGEVLIRV HAIGVNPPDW
YLRDGYKMLP PEWRPQVPFP IILGSDVSGI VVAVAQDVTD FSAGDEVFGM VRFPSVGESA
AYAQYVAAPA TDLALKPSGL DHIHAAASAM AGLTAWQFLI ELGHNHPNPL QAEMHQPLPL
KDKTILINGA AGGVGHFAVQ LAKWKGANVT AVASTTHESF LRDLGANHFI DYTKTPPEDV
AHNIDIVLDT LGGANTGRFL KTIKPGGALF PVFLGFSDHD EAAKLDITVS MTQVRSNGLQ
LFELAKLLEA GTIKVAIDST FTLSDAKSAH ERAANGHIQG KIVLIVD
//
