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Database: UniProt
Entry: S3NLK7_9GAMM
LinkDB: S3NLK7_9GAMM
Original site: S3NLK7_9GAMM 
ID   S3NLK7_9GAMM            Unreviewed;       331 AA.
AC   S3NLK7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=NADPH2:quinone reductase {ECO:0000313|EMBL:EPF80582.1};
GN   ORFNames=F945_00323 {ECO:0000313|EMBL:EPF80582.1};
OS   Acinetobacter rudis CIP 110305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF80582.1, ECO:0000313|Proteomes:UP000014568};
RN   [1] {ECO:0000313|EMBL:EPF80582.1, ECO:0000313|Proteomes:UP000014568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF80582.1,
RC   ECO:0000313|Proteomes:UP000014568};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL   Submitted (JUN-2013) 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:EPF80582.1}.
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DR   EMBL; ATGI01000003; EPF80582.1; -; Genomic_DNA.
DR   RefSeq; WP_016654771.1; NZ_KE340348.1.
DR   AlphaFoldDB; S3NLK7; -.
DR   STRING; 632955.GCA_000829675_00067; -.
DR   PATRIC; fig|421052.3.peg.323; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_026673_3_1_6; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000014568; Unassembled WGS sequence.
DR   GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05286; QOR2; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047618; QOR-like.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1.
DR   PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-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; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014568}.
FT   DOMAIN          13..326
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   331 AA;  35520 MW;  6C1F14D58CA5D598 CRC64;
     MTMIKAVRFY ETGTAEVMRY EDAEIGQPAA GEVLLRHVAV GLNYADTYFR NGTYQIPLPN
     GMGVEAAGVI EAVGEGVTDF VVGDRVTYTG FLNTLGAYST QRLIAANALI KLPDAISCET
     AAAMTMRGLT SAYLMRRIYD FKAGDSILLH AAAGGVGLIV AQWAKILGLT VIGTTSSTAK
     AEIARAHGCD HVINYSHENV AQRVRELTNG TGVNVVFDSV GKDTFMASLD SLKRRGLLVC
     VGTASGPIPA FDPVLLAMKG SLYVTRPALA DYIADPAEKK ALAAELFEHV AQGRIKIEIN
     QRYKLEDAVQ AHRDLEARKT TGSSIFVIEQ S
//
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