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
//