ID Q9I377_PSEAE Unreviewed; 334 AA. AC Q9I377; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 124. DE SubName: Full=Probable oxidoreductase {ECO:0000313|EMBL:AAG05037.1}; GN OrderedLocusNames=PA1648 {ECO:0000313|EMBL:AAG05037.1}; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG05037.1, ECO:0000313|Proteomes:UP000002438}; RN [1] {ECO:0000313|EMBL:AAG05037.1, ECO:0000313|Proteomes:UP000002438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438}; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K., RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H., RA Hancock R.E., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [2] {ECO:0007829|PDB:4B7C, ECO:0007829|PDB:4B7X} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP(+). RX PubMed=23295481; DOI=10.1107/S1744309112044739; RA Moynie L., Schnell R., McMahon S.A., Sandalova T., Boulkerou W.A., RA Schmidberger J.W., Alphey M., Cukier C., Duthie F., Kopec J., Liu H., RA Jacewicz A., Hunter W.N., Naismith J.H., Schneider G.; RT "The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic RT studies for assessment of potential targets in early-stage drug RT discovery."; RL Acta Crystallogr. F Struct. Biol. Commun. 69:25-34(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG05037.1; -; Genomic_DNA. DR PIR; E83440; E83440. DR RefSeq; NP_250339.1; NC_002516.2. DR RefSeq; WP_003097826.1; NZ_QZGE01000003.1. DR PDB; 4B7C; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-334. DR PDB; 4B7X; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-334. DR PDBsum; 4B7C; -. DR PDBsum; 4B7X; -. DR AlphaFoldDB; Q9I377; -. DR SMR; Q9I377; -. DR STRING; 208964.PA1648; -. DR PaxDb; 208964-PA1648; -. DR GeneID; 882158; -. DR KEGG; pae:PA1648; -. DR PATRIC; fig|208964.12.peg.1709; -. DR PseudoCAP; PA1648; -. DR HOGENOM; CLU_026673_29_2_6; -. DR InParanoid; Q9I377; -. DR OrthoDB; 9805663at2; -. DR PhylomeDB; Q9I377; -. DR BioCyc; PAER208964:G1FZ6-1679-MONOMER; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR CDD; cd05288; PGDH; 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; IPR041694; ADH_N_2. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR045010; MDR_fam. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1. DR PANTHER; PTHR43205:SF7; PROSTAGLANDIN REDUCTASE 1; 1. DR Pfam; PF16884; ADH_N_2; 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4B7C, ECO:0007829|PDB:4B7X}; KW Nucleotide-binding {ECO:0007829|PDB:4B7X}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000002438}. FT DOMAIN 20..332 FT /note="Enoyl reductase (ER)" FT /evidence="ECO:0000259|SMART:SM00829" FT BINDING 159 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 160 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 180 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 184 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 200 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 223 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 245 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 251 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 276 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 278 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" FT BINDING 326 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:4B7X" SQ SEQUENCE 334 AA; 36169 MW; 8294AD44FEA5CE43 CRC64; MTSQINRQYQ LAQRPSGLPG RDTFSFVETP LGEPAEGQIL VKNEYLSLDP AMRGWMNDAR SYIPPVGIGE VMRALGVGKV LVSKHPGFQA GDYVNGALGV QDYFIGEPKG FYKVDPSRAP LPRYLSALGM TGMTAYFALL DVGQPKNGET VVISGAAGAV GSVAGQIARL KGCRVVGIAG GAEKCRFLVE ELGFDGAIDY KNEDLAAGLK RECPKGIDVF FDNVGGEILD TVLTRIAFKA RIVLCGAISQ YNNKEAVRGP ANYLSLLVNR ARMEGMVVMD YAQRFPEGLK EMATWLAEGK LQSREDIVEG LETFPETLLK LFSGENFGKL VLKV //