ID A0A1W6NXU8_9RHOB Unreviewed; 675 AA.
AC A0A1W6NXU8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=hppD {ECO:0000313|EMBL:ARO13847.1};
GN ORFNames=BVG79_00493 {ECO:0000313|EMBL:ARO13847.1};
OS Ketogulonicigenium robustum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ketogulonicigenium.
OX NCBI_TaxID=92947 {ECO:0000313|EMBL:ARO13847.1, ECO:0000313|Proteomes:UP000242447};
RN [1] {ECO:0000313|EMBL:ARO13847.1, ECO:0000313|Proteomes:UP000242447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPU_B003 {ECO:0000313|EMBL:ARO13847.1,
RC ECO:0000313|Proteomes:UP000242447};
RA Li Y., Liu L., Wang C., Zhang M., Zhang T., Zhang Y.;
RT "Ketogulonicigenium robustum SPU B003 Genome sequencing and assembly.";
RL Submitted (FEB-2017) 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; CP019937; ARO13847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6NXU8; -.
DR STRING; 92947.BVG79_00493; -.
DR KEGG; kro:BVG79_00493; -.
DR UniPathway; UPA00088; -.
DR Proteomes; UP000242447; Chromosome.
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; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:ARO13847.1};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02238};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02238};
KW Oxidoreductase {ECO:0000313|EMBL:ARO13847.1};
KW Pyruvate {ECO:0000313|EMBL:ARO13847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242447}.
FT DOMAIN 484..631
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 182
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 213
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 287
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 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 563
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 640
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
SQ SEQUENCE 675 AA; 73043 MW; A1981E67EE693E1E CRC64;
MMRAQAATIR PETASAAAAA TPLAKTTLYD LQIIWCYSFR MLQSDWTAMK TSIATVSISG
TFQDKLAAIA AAGFDGIEIF EQDFLASDLS PRDAARMVRD FGLEIMLFQP FRDFEGLPAP
LRQRAFSRAE HKFDLMAELG TDLALFCSSL HPAAIGGIDR AADDFHALGD IARQRGIRVG
YEALCWGKHV SDHRDAWEIV RRADHDNIGL ILDSFHTLGP KIDPETIRRI PGDKIFFVQL
ADAPAIPMDL LYWSRHFRNM PGEGDLDVTA FTRAILATGY DGPLSLEIFN DQFRAGLPRL
VAQSGYRSLV ALMDRVARAE PALATNLPAI PPPAQVSAVE FLEFATTAPE AAPLEATLKA
AGFAQAGAHR SKAVSLWRQG DISLLINTSS DDFNLTSWST HGTTVSEIGL KVPSAAASAQ
RAQALGAKPH TSAAPAPGER AFPGIRHAGG SVLRFLDDAN GAPSIWQSDF TVAQGTPAGI
GLTHIDHIAQ TMAYDEMLSW SLFYTTLLDA ARAPMVDVID PDGLVRSQAL AAGALRVTLN
GAEARRTLAG QFIEETYGAS VQHIAFATTD IFATAEALAS RAFPVLPIGG NYYGDLAARF
DLPTADLQRM QALNILYDED ENGRFWQIFS RPLAGGLFLE FVQRDGGYAG YGGPNAPFRI
AAMKRQMRPA GMPKA
//
