PHZS_PSEAE
ID PHZS_PSEAE Reviewed; 402 AA.
AC Q9HWG9;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=5-methylphenazine-1-carboxylate 1-monooxygenase {ECO:0000305};
DE EC=1.14.13.218 {ECO:0000269|PubMed:17253782};
GN Name=phzS {ECO:0000303|PubMed:17012792};
GN OrderedLocusNames=PA4217 {ECO:0000312|EMBL:AAG07605.1};
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, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=17253782; DOI=10.1021/bi6024403;
RA Parsons J.F., Greenhagen B.T., Shi K., Calabrese K., Robinson H.,
RA Ladner J.E.;
RT "Structural and functional analysis of the pyocyanin biosynthetic protein
RT PhzM from Pseudomonas aeruginosa.";
RL Biochemistry 46:1821-1828(2007).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=17012792; DOI=10.1107/s1744309106034464;
RA Gohain N., Thomashow L.S., Mavrodi D.V., Blankenfeldt W.;
RT "The purification, crystallization and preliminary structural
RT characterization of FAD-dependent monooxygenase PhzS, a phenazine-modifying
RT enzyme from Pseudomonas aeruginosa.";
RL Acta Crystallogr. F 62:989-992(2006).
RN [4] {ECO:0007744|PDB:2RGJ}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FAD, AND COFACTOR.
RX PubMed=18416536; DOI=10.1021/bi702480t;
RA Greenhagen B.T., Shi K., Robinson H., Gamage S., Bera A.K., Ladner J.E.,
RA Parsons J.F.;
RT "Crystal structure of the pyocyanin biosynthetic protein PhzS.";
RL Biochemistry 47:5281-5289(2008).
RN [5] {ECO:0007744|PDB:3C96}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD, AND COFACTOR.
RG Northeast structural genomics consortium (NESG);
RA Vorobiev S.M., Chen Y., Seetharaman J., Wang D., Mao L., Xiao R.,
RA Acton T.B., Montelione G.T., Tong L., Hunt J.F.;
RT "Crystal structure of the flavin-containing monooxygenase phzS from
RT Pseudomonas aeruginosa.";
RL Submitted (FEB-2008) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of pyocyanine, a blue-pigmented
CC phenazine derivative, which plays a role in virulence. Catalyzes the
CC oxidative decarboxylation of 5-methylphenazine-1-carboxylate (5-methyl-
CC PCA) to pyocyanine. Can also act on phenazine-1-carboxylate (PCA),
CC converting it into 1-hydroxyphenazine (1-HP). However, PCA is a poor
CC substrate. {ECO:0000269|PubMed:17253782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyl-phenazine-1-carboxylate + 2 H(+) + NADH + O2 = CO2 +
CC H2O + NAD(+) + pyocyanin; Xref=Rhea:RHEA:48976, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62220,
CC ChEBI:CHEBI:62221; EC=1.14.13.218;
CC Evidence={ECO:0000269|PubMed:17253782};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5};
CC -!- PATHWAY: Secondary metabolite biosynthesis; pyocyanine biosynthesis.
CC {ECO:0000269|PubMed:17253782}.
CC -!- SUBUNIT: Monomer in solution. Probably interacts transiently with PhzM.
CC {ECO:0000269|PubMed:17253782}.
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; AAG07605.1; -; Genomic_DNA.
DR PIR; E83119; E83119.
DR RefSeq; NP_252907.1; NC_002516.2.
DR RefSeq; WP_003115086.1; NZ_QZGE01000042.1.
DR PDB; 2RGJ; X-ray; 2.40 A; A=1-402.
DR PDB; 3C96; X-ray; 1.90 A; A=1-402.
DR PDBsum; 2RGJ; -.
DR PDBsum; 3C96; -.
DR AlphaFoldDB; Q9HWG9; -.
DR SMR; Q9HWG9; -.
DR STRING; 287.DR97_3694; -.
DR PaxDb; Q9HWG9; -.
DR PRIDE; Q9HWG9; -.
DR DNASU; 881836; -.
DR EnsemblBacteria; AAG07605; AAG07605; PA4217.
DR GeneID; 881836; -.
DR KEGG; pae:PA4217; -.
DR PATRIC; fig|208964.12.peg.4418; -.
DR PseudoCAP; PA4217; -.
DR HOGENOM; CLU_009665_19_5_6; -.
DR InParanoid; Q9HWG9; -.
DR OMA; EYPMVDR; -.
DR PhylomeDB; Q9HWG9; -.
DR BioCyc; MetaCyc:MON-16022; -.
DR BioCyc; PAER208964:G1FZ6-4290-MON; -.
DR BRENDA; 1.14.13.218; 5087.
DR UniPathway; UPA00235; -.
DR EvolutionaryTrace; Q9HWG9; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:PseudoCAP.
DR GO; GO:0102169; F:pyocyanin hydroxylase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Monooxygenase; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..402
FT /note="5-methylphenazine-1-carboxylate 1-monooxygenase"
FT /id="PRO_0000441708"
FT REGION 368..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT BINDING 43..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT BINDING 106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18416536, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2RGJ, ECO:0007744|PDB:3C96"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 125..138
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 183..197
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:3C96"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2RGJ"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:3C96"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 323..339
FT /evidence="ECO:0007829|PDB:3C96"
FT HELIX 343..377
FT /evidence="ECO:0007829|PDB:3C96"
SQ SEQUENCE 402 AA; 43645 MW; F2BB36662ABAC790 CRC64;
MSEPIDILIA GAGIGGLSCA LALHQAGIGK VTLLESSSEI RPLGVGINIQ PAAVEALAEL
GLGPALAATA IPTHELRYID QSGATVWSEP RGVEAGNAYP QYSIHRGELQ MILLAAVRER
LGQQAVRTGL GVERIEERDG RVLIGARDGH GKPQALGADV LVGADGIHSA VRAHLHPDQR
PLSHGGITMW RGVTEFDRFL DGKTMIVAND EHWSRLVAYP ISARHAAEGK SLVNWVCMVP
SAAVGQLDNE ADWNRDGRLE DVLPFFADWD LGWFDIRDLL TRNQLILQYP MVDRDPLPHW
GRGRITLLGD AAHLMYPMGA NGASQAILDG IELAAALARN ADVAAALREY EEARRPTANK
IILANREREK EEWAAASRPK TEKSAALEAI TGSYRNQVER PR
