DSD_PSEAE
ID DSD_PSEAE Reviewed; 634 AA.
AC Q9I6P6;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=3-dehydroshikimate dehydratase {ECO:0000303|PubMed:27706847};
DE Short=DSD {ECO:0000303|PubMed:27706847};
DE EC=4.2.1.118 {ECO:0000305|PubMed:27706847};
GN Name=quiC1 {ECO:0000303|PubMed:27706847};
GN OrderedLocusNames=PA0242 {ECO:0000312|EMBL:AAG03631.1};
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, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27706847; DOI=10.1111/mmi.13542;
RA Peek J., Roman J., Moran G.R., Christendat D.;
RT "Structurally diverse dehydroshikimate dehydratase variants participate in
RT microbial quinate catabolism.";
RL Mol. Microbiol. 103:39-54(2017).
CC -!- FUNCTION: Catalyzes the conversion of 3-dehydroshikimate to
CC protocatechuate (3,4-dihydroxybenzoate), a common intermediate of
CC quinate and shikimate degradation pathways. Is required for growth on
CC either quinate or shikimate as a sole carbon source.
CC {ECO:0000269|PubMed:27706847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O;
CC Xref=Rhea:RHEA:24848, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36241; EC=4.2.1.118;
CC Evidence={ECO:0000305|PubMed:27706847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24849;
CC Evidence={ECO:0000269|PubMed:27706847};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q88JU3};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q88JU3};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q88JU3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q88JU3};
CC Note=Requires a divalent metal cation for DSD activity, with a
CC preference for Co(2+) but can also use Ni(2+), Mn(2+) and Mg(2+).
CC {ECO:0000250|UniProtKB:Q88JU3};
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis. {ECO:0000269|PubMed:27706847}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q88JU3}.
CC -!- DOMAIN: Consists of a fusion of two distinct domains: an N-terminal
CC sugar phosphate isomerase-like domain associated with DSD activity and
CC a C-terminal hydroxyphenyl-pyruvate dioxygenase-like domain. This C-
CC terminal domain does not show any 4-hydroxyphenylpyruvate dioxygenase
CC (HPPD) or protocatechuate dioxygenase (PCD) activity, but appears to be
CC important for optimal DSD activity of QuiC1 in vivo.
CC {ECO:0000250|UniProtKB:Q88JU3}.
CC -!- DISRUPTION PHENOTYPE: While wild-type P.aeruginosa grows readily on
CC either quinate or shikimate as a sole carbon source, the knockout
CC strain does not efficiently utilize these substrates. Growth of the
CC knockout is enhanced by the addition of protocatechuate, bypassing the
CC function of QuiC1. {ECO:0000269|PubMed:27706847}.
CC -!- SIMILARITY: Belongs to the bacterial two-domain DSD family.
CC {ECO:0000255|HAMAP-Rule:MF_02238, ECO:0000305|PubMed:27706847}.
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; AAG03631.1; -; Genomic_DNA.
DR PIR; D83615; D83615.
DR RefSeq; NP_248933.1; NC_002516.2.
DR RefSeq; WP_003112679.1; NZ_QZGE01000024.1.
DR AlphaFoldDB; Q9I6P6; -.
DR SMR; Q9I6P6; -.
DR STRING; 287.DR97_3199; -.
DR PaxDb; Q9I6P6; -.
DR EnsemblBacteria; AAG03631; AAG03631; PA0242.
DR GeneID; 880907; -.
DR KEGG; pae:PA0242; -.
DR PATRIC; fig|208964.12.peg.252; -.
DR PseudoCAP; PA0242; -.
DR HOGENOM; CLU_029438_0_0_6; -.
DR InParanoid; Q9I6P6; -.
DR OMA; FPGQGEF; -.
DR PhylomeDB; Q9I6P6; -.
DR BioCyc; PAER208964:G1FZ6-244-MON; -.
DR UniPathway; UPA00088; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0046565; F:3-dehydroshikimate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019631; P:quinate catabolic process; IMP:UniProtKB.
DR GO; GO:0019633; P:shikimate catabolic process; IMP:UniProtKB.
DR CDD; cd08342; HPPD_N_like; 1.
DR Gene3D; 3.10.180.10; -; 2.
DR HAMAP; MF_02238; DSD; 1.
DR InterPro; IPR041736; 4OHPhenylPyrv_dOase_N.
DR InterPro; IPR043700; DSD.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR PROSITE; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Cobalt; Lyase; Magnesium; Manganese; Metal-binding; Nickel;
KW Reference proteome.
FT CHAIN 1..634
FT /note="3-dehydroshikimate dehydratase"
FT /id="PRO_0000448877"
FT DOMAIN 295..414
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 440..590
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
FT BINDING 191
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
FT BINDING 239
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q88JU3"
SQ SEQUENCE 634 AA; 70216 MW; 0ED28FB17EBF9009 CRC64;
MQRSIATVSL SGTLPEKLEA IAAAGFDGVE IFENDLLHYD GSPRDVRRLC ADLGLEILLF
QPFRDFEGCR RERLGRNLER AERKFDLMQE LGTDLVLVCS NVAADALGEP ALLADDLRQL
AERAAVRGLR IGYEALAWGR QVNTWEQAWD LVRRADQANL GLILDSFHTL SLDGDPRGIA
DLPGEKIFFV QMADAPLLAM DVLEWSRHFR CFPGQGGFDL AGFLAPVVAS GYRGPLSLEV
FNDGFRAAPT RANAVDGLRS LLYLEEKTRE HLQRQTPHVA VDELFAPPPA SLCDGIEFLE
FAVDETLGAR LGQWLQRLGF ARAGEHRSKN VSLLRQGDIN LVLNAEPYSF AHGFFEAHGP
SLCATALCVR DAGQALERAR AYGGQPYRGL LGPNEREIPA VRALDGSLLY LVERHTEGRS
IYDSDFVTND ADTSGLGLRR VDHVALALPA EGLDSWVLFY KSLFDFGADD EVVLPDPYGL
VTSRAVRSPC GSVRLPLNIS EDRNTAIARS LSSYRGSGVH HIAFDCADIF AAVAQAKEAG
VALLEIPLNY YDDLAARFDF DDEFLSELAY YNVLYDRDAQ GGELFHVFTE PFEERFFFEI
LQRRHGYAGY GAANVPVRLA AMAQARRGVR RVKL
