ID A0A1I2GJU5_9BURK Unreviewed; 641 AA.
AC A0A1I2GJU5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=3-dehydroshikimate dehydratase {ECO:0000256|HAMAP-Rule:MF_02238};
DE Short=DSD {ECO:0000256|HAMAP-Rule:MF_02238};
DE EC=4.2.1.118 {ECO:0000256|HAMAP-Rule:MF_02238};
GN ORFNames=SAMN04489711_11535 {ECO:0000313|EMBL:SFF17006.1};
OS Paracidovorax wautersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=1177982 {ECO:0000313|EMBL:SFF17006.1, ECO:0000313|Proteomes:UP000199119};
RN [1] {ECO:0000313|EMBL:SFF17006.1, ECO:0000313|Proteomes:UP000199119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27981 {ECO:0000313|EMBL:SFF17006.1,
RC ECO:0000313|Proteomes:UP000199119};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 3-dehydroshikimate to
CC protocatechuate (3,4-dihydroxybenzoate), a common intermediate of
CC quinate and shikimate degradation pathways. {ECO:0000256|HAMAP-
CC Rule:MF_02238}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02238};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02238};
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02238}.
CC -!- SIMILARITY: Belongs to the bacterial two-domain DSD family.
CC {ECO:0000256|HAMAP-Rule:MF_02238}.
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DR EMBL; FONX01000015; SFF17006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2GJU5; -.
DR STRING; 1177982.SAMN04489711_11535; -.
DR OrthoDB; 9780241at2; -.
DR UniPathway; UPA00088; -.
DR Proteomes; UP000199119; Unassembled WGS sequence.
DR GO; GO:0046565; F:3-dehydroshikimate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR HAMAP; MF_02238; DSD; 1.
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 PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1.
DR PANTHER; PTHR12110:SF21; XYLOSE ISOMERASE-LIKE TIM BARREL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR Pfam; PF14696; Glyoxalase_5; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:SFF17006.1};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02238};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02238};
KW Oxidoreductase {ECO:0000313|EMBL:SFF17006.1};
KW Pyruvate {ECO:0000313|EMBL:SFF17006.1}.
FT DOMAIN 308..427
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 457..619
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 191
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 239
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
SQ SEQUENCE 641 AA; 68989 MW; 9B15A8F3DDC91587 CRC64;
MHRSIATVSL SGTLRQKLEA VAAAGFDGIE LFEADFIHFQ GSAAELRRIA ADLGLSIDLY
QPLRDMEGLP DAAFARALER AERKFDLMQE LGAPLVLCCS NTLAHSIDDP DLAAAQLHTL
AERAARRNLR VGYEALAWGR HTSRFGQAWD IVRRADHPHL GLILDSFHTL SLRDDPAPIA
AIPGDRIFFV QMADAPLMSL DVLQWARHYR VFPGQGDFDV IGFFEQVLRA GYTGPLSLEI
FNDLFRETPN RRTAVDAMRS LLYLESEARQ RLAIPQAASL DAAAPATASA PPLRVELFNP
PPAPTFQGVS FIEFAADEAA AEALDGVLRG LGFARVGQHR SKAATLYRQG GIHLIVNAQP
DSFARSRFAL HGTSVCALGL RCDDAIGALG RAKAMRSQPY DSPLGPQEQR VPATVAPGGN
LIHFVPAALG TDGLFEADFV LDAAAQADAG PTPGLQSVDH LTLGLGQDQR DTWALFTRAV
LGLDCMESLD LADPFGLVRS QGVANAERSL RLVLNVPLSQ RTATARQLGV TGAGAVHHIT
FGCDDIFAAV AALRARGVRF EPVSGNYYDD LQARLDLAPG LLERLRAAGV LFDRSPAGDY
LHAYTEGLPG GLFFEIAQRV GGYDGWGAAN AAARLASLAQ R
//
