PANE_PSEAE
ID PANE_PSEAE Reviewed; 303 AA.
AC Q9HW09;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:P0A9J4};
DE EC=1.1.1.169 {ECO:0000250|UniProtKB:P0A9J4};
DE AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:P0A9J4};
DE Short=KPR {ECO:0000250|UniProtKB:P0A9J4};
GN Name=panE; OrderedLocusNames=PA4397;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., 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.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., 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:0007744|PDB:5ZIK}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RA Khanppnavar B., Datta S.;
RT "Crystal structure of ketopantoate reductase from Pseudomonas aeruginosa.";
RL Submitted (MAR-2018) to the PDB data bank.
RN [3] {ECO:0007744|PDB:5ZIX}
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH NADP.
RA Khanppnavar B., Datta S.;
RT "Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa
RT bound to NADP+.";
RL Submitted (MAR-2018) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
CC Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.169; Evidence={ECO:0000250|UniProtKB:P0A9J4};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG07785.1; -; Genomic_DNA.
DR PIR; E83096; E83096.
DR RefSeq; NP_253087.1; NC_002516.2.
DR RefSeq; WP_003106518.1; NZ_QZGE01000004.1.
DR PDB; 5ZIK; X-ray; 2.45 A; A/B/C=1-303.
DR PDB; 5ZIX; X-ray; 2.57 A; A/B/C=1-303.
DR PDB; 6K1R; X-ray; 2.55 A; A/B/C=1-303.
DR PDBsum; 5ZIK; -.
DR PDBsum; 5ZIX; -.
DR PDBsum; 6K1R; -.
DR AlphaFoldDB; Q9HW09; -.
DR SMR; Q9HW09; -.
DR STRING; 287.DR97_1575; -.
DR PaxDb; Q9HW09; -.
DR PRIDE; Q9HW09; -.
DR EnsemblBacteria; AAG07785; AAG07785; PA4397.
DR GeneID; 881354; -.
DR KEGG; pae:PA4397; -.
DR PATRIC; fig|208964.12.peg.4605; -.
DR PseudoCAP; PA4397; -.
DR HOGENOM; CLU_031468_0_1_6; -.
DR InParanoid; Q9HW09; -.
DR OMA; NYSSMYQ; -.
DR PhylomeDB; Q9HW09; -.
DR BioCyc; PAER208964:G1FZ6-4483-MON; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR003710; ApbA.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00745; apbA_panE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Oxidoreductase; Pantothenate biosynthesis;
KW Reference proteome.
FT CHAIN 1..303
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157308"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 7..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 129
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 262
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:5ZIK"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 175..196
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 227..243
FT /evidence="ECO:0007829|PDB:5ZIK"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:5ZIK"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:5ZIK"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5ZIK"
SQ SEQUENCE 303 AA; 33062 MW; 664A30DF3028E1D8 CRC64;
MTWHILGAGS LGSLWAARLG RAGLPVRLIL RDRQRLRRYQ QAGGLSLVED GQASLYPIAA
ETPDGGQPIQ RLLLACKAYD AEEAASSVAH RLAGNAELLL LQNGLGSQQA VAARLPRSRC
LFASSTEGAF RDGDFRVVFA GRGHTWLGDP RDTNAPAWLT QLSQAGIPHS WSDDILERLW
RKLALNCAIN PLTVLHDCRN GGLRQHPEEI AALCDELGQL LHASGYDAAA RSLLEDVRAV
IDATAANYSS MHQDVTRGRR TEIGYLLGYA CQHGQRLGLP LPRLGTLLAR LQAHLRQRGL
PDR
