ID A0A1M7TT04_9RHOB Unreviewed; 629 AA.
AC A0A1M7TT04;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216200_109115 {ECO:0000313|EMBL:SHN73851.1};
OS Oceanicella actignis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Oceanicella.
OX NCBI_TaxID=1189325 {ECO:0000313|EMBL:SHN73851.1, ECO:0000313|Proteomes:UP000184066};
RN [1] {ECO:0000313|EMBL:SHN73851.1, ECO:0000313|Proteomes:UP000184066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10808 {ECO:0000313|EMBL:SHN73851.1,
RC ECO:0000313|Proteomes:UP000184066};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; FRDL01000009; SHN73851.1; -; Genomic_DNA.
DR RefSeq; WP_072748057.1; NZ_VNHJ01000009.1.
DR AlphaFoldDB; A0A1M7TT04; -.
DR STRING; 1189325.SAMN04488119_1097; -.
DR OrthoDB; 9780241at2; -.
DR UniPathway; UPA00088; -.
DR Proteomes; UP000184066; 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; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:SHN73851.1};
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:SHN73851.1};
KW Pyruvate {ECO:0000313|EMBL:SHN73851.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184066}.
FT DOMAIN 436..585
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 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 517
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 594
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
SQ SEQUENCE 629 AA; 69358 MW; 763FEFCFB32622F1 CRC64;
MKTSIATVSI SGSLREKLAA ISKIGFDGIE IFEQDFIADE GSPREIGRMI RDHGLEITLF
QPFRDFEGLT GEARRRAFDR ARCKFDTMVE LGAELLLVCS SVHPESLGGI DRAAQDLAEL
GDIAAERGLR VGYEALAWGR HVNDHRDAWE IVRRADHPNV GLILDSFHTL ARKIDPNTIR
RIPGDRIFFV QLADAPQIEM DLLYWSRHFR CMPGEGDLPV QAFMQAVAAT GYDGPVSLEI
FNDQFRGGRP EGLARDGYRS LAALMDDVRR AEPDIRIKVP DMPARVAAQG VAFIEFATRG
EEAEALAKLL HCMGFRHVGD HVSKRVALWR QGEARVVVNA ETEGFANSAY LVHGTTVCDV
GLSVSSAADT VARALALAAE PFEQPVGPGE MKIPAIRSVG GSVMHFIDQV SGLSDVWSVE
FRGSGEAKPG GAGLTRIDHV AETMNYDEML SWSLFYTSIF DMERTPMVDV VDPDGLVRSQ
AIKSRDGRTR ITLNGAETHR TLAGSFLAES FGGAVQHVAF ATDDIFATAR AMADLGFEPL
PMTVNYYHDL RARFGLEPSR VEELMAFNIL YDEDADGAFF QFYSRPFAEG LFFEVVQRVG
GYDGYGAANA PFRIAAQKRL MRPKGVPRK
//
