Y4991_PSEAE
ID Y4991_PSEAE Reviewed; 391 AA.
AC Q9HUH4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable FAD-dependent oxidoreductase PA4991 {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
GN OrderedLocusNames=PA4991 {ECO:0000312|EMBL:AAG08376.1};
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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=25775563; DOI=10.1073/pnas.1419677112;
RA Turner K.H., Wessel A.K., Palmer G.C., Murray J.L., Whiteley M.;
RT "Essential genome of Pseudomonas aeruginosa in cystic fibrosis sputum.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4110-4115(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26841760; DOI=10.1107/s2053230x15024437;
RA Jacewicz A., Schnell R., Lindqvist Y., Schneider G.;
RT "Crystal structure of the flavoenzyme PA4991 from Pseudomonas aeruginosa.";
RL Acta Crystallogr. F Struct. Biol. Commun. 72:105-111(2016).
CC -!- FUNCTION: Probably functions as a FAD-dependent oxidoreductase, whose
CC physiological substrate is unknown. Does not display amino-acid oxidase
CC or glycerol-3-phosphate dehydrogenase activities (PubMed:26841760). Is
CC essential for growth of P.aeruginosa in the sputum of cystic fibrosis
CC patients (PubMed:25775563). {ECO:0000269|PubMed:25775563,
CC ECO:0000269|PubMed:26841760}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:26841760};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:26841760};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26841760}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show growth defect in
CC natural and synthetic cystic fibrosis sputum.
CC {ECO:0000269|PubMed:25775563}.
CC -!- SIMILARITY: Belongs to the DAO family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08376.1; -; Genomic_DNA.
DR PIR; D83021; D83021.
DR RefSeq; NP_253678.1; NC_002516.2.
DR RefSeq; WP_003114540.1; NZ_QZGE01000002.1.
DR PDB; 5EZ7; X-ray; 2.40 A; A=1-391.
DR PDBsum; 5EZ7; -.
DR AlphaFoldDB; Q9HUH4; -.
DR SMR; Q9HUH4; -.
DR STRING; 287.DR97_2345; -.
DR PaxDb; Q9HUH4; -.
DR PRIDE; Q9HUH4; -.
DR DNASU; 880166; -.
DR EnsemblBacteria; AAG08376; AAG08376; PA4991.
DR GeneID; 880166; -.
DR KEGG; pae:PA4991; -.
DR PATRIC; fig|208964.12.peg.5231; -.
DR PseudoCAP; PA4991; -.
DR HOGENOM; CLU_705707_0_0_6; -.
DR OMA; WPTKLAL; -.
DR PhylomeDB; Q9HUH4; -.
DR BioCyc; PAER208964:G1FZ6-5107-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..391
FT /note="Probable FAD-dependent oxidoreductase PA4991"
FT /id="PRO_0000439959"
FT BINDING 17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26841760"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26841760"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26841760"
FT BINDING 49..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26841760"
FT BINDING 346..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26841760"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5EZ7"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 284..298
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 308..319
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5EZ7"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:5EZ7"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:5EZ7"
SQ SEQUENCE 391 AA; 42109 MW; D2614EA26F47A949 CRC64;
MPQALSTDIL IVGGGIAGLW LNARLRRAGY ATVLVESASL GGGQSVKSQG IIHGGAKYAL
HGALTGASEA IADMPRRWRA CLGSDGELDL RGVRLLSEAH YLWSPGGLAG SLTSFFASKA
VRSRVEQAKG EDLPPALRDK GFKGKAYRLT EIVFDVPDLI RRLAELAGDS LLAGERIEPL
REGRELAGLC VDGREIRAQR VVLSAGAGNE ALLRELGLEQ PAMQRRPLHM VMVKAATLKP
LYAHCLGAGP KPRITVTTHP TRDGQSVWYL GGDIAETDGV ARDEAAQIAE ARRELAKLLP
WIDLGQAQWA TLRVDRAEPA QSNLLRPDNA FLAEQGRLLV GWPTKLALAP DFADRVCARL
EEDGIRPSEH AALPQLPRPP LAEPAWEVAF A
