ID A0A0P1GCH1_9RHOB Unreviewed; 627 AA.
AC A0A0P1GCH1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 Name=hpd_2 {ECO:0000313|EMBL:CUH79075.1};
GN ORFNames=TRN7648_02314 {ECO:0000313|EMBL:CUH79075.1};
OS Tropicibacter naphthalenivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicibacter.
OX NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH79075.1, ECO:0000313|Proteomes:UP000054935};
RN [1] {ECO:0000313|EMBL:CUH79075.1, ECO:0000313|Proteomes:UP000054935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH79075.1,
RC ECO:0000313|Proteomes:UP000054935};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSE01000003; CUH79075.1; -; Genomic_DNA.
DR RefSeq; WP_058247780.1; NZ_FWXX01000011.1.
DR AlphaFoldDB; A0A0P1GCH1; -.
DR STRING; 441103.TRN7648_02314; -.
DR OrthoDB; 9780241at2; -.
DR UniPathway; UPA00088; -.
DR Proteomes; UP000054935; 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 CDD; cd08342; HPPD_N_like; 1.
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; 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 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:CUH79075.1};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02238};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02238}; Oxidoreductase {ECO:0000313|EMBL:CUH79075.1};
KW Pyruvate {ECO:0000313|EMBL:CUH79075.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054935}.
FT DOMAIN 289..408
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 432..581
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 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 513
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
SQ SEQUENCE 627 AA; 68665 MW; 80DBC0467B3688C0 CRC64;
MKTSIATVSI SGTLTEKLRA IADAGFDGIE IFEADFIAHD GAPRDVGNMI RDHGLDITLF
QPFRDFEGLP APLRAKAFDR AERKFDLMQE LGTDLVLICS SCHPASLGGI DRCADDFAEL
GERAAKRGLR VGYEALAWGR HINDHRDAWE IVRRADHPNV GLILDSFHTL GRKLSPESIR
AIPADRIFFV QLADAPQIEM DLLYWSRHFR NMPGEGDLDV TAFMRAVMAT GYAGPISLEI
FNDQFRGGDT KLLAGDGHRS LLTLMDDVRR AEPVAVDLPV MPARVAAKGV SFIEFASRGA
EAQTLSNQLQ TLGFRKAAKH RNKALTLFQQ GDVRIVLNEE TTGYAATAWT ARGTTICDIG
LRTASARDAI ARATALGAQP FEQPLGPGEL NIPAIRGLSG SVLHMMDDDL ADVWQVEFAP
LDAPDVDAGL TRVDHLAQTM SYDDMLSWSL FYTSLFDLAK TPMVDVIDPD GLVRSQALST
PGGDLRITLN GADSHRTLAG RLLSDTFGAP LQHVALACDD IVKTADKLAA RGFEALNMPA
NYYDDLASRF DLTSEKLDAL RRRNILYDED AQGAFYQIYS RDFAGGLFFE ILQREGDYQG
YGGPNAPFRI AAQKRLMRAK GVPGDAG
//
