ID A0A0M8VIV7_9ACTN Unreviewed; 602 AA.
AC A0A0M8VIV7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-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 ORFNames=ADL00_17455 {ECO:0000313|EMBL:KOV66689.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV66689.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV66689.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV66689.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOV66689.1}.
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DR EMBL; LGDU01000163; KOV66689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8VIV7; -.
DR PATRIC; fig|1519489.3.peg.3973; -.
DR UniPathway; UPA00088; -.
DR Proteomes; UP000037758; 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:SF21; DEHYDRATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08740)-RELATED; 1.
DR PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 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:KOV66689.1};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02238};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02238};
KW Oxidoreductase {ECO:0000313|EMBL:KOV66689.1};
KW Pyruvate {ECO:0000313|EMBL:KOV66689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037758}.
FT DOMAIN 272..383
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 422..562
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 125
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 156
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 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 230
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 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02238"
SQ SEQUENCE 602 AA; 64899 MW; 1F665C5BB6145B2D CRC64;
MSGSLTEKLT AASRAGFDGV EIFENDLLAA PLTPEEIRAR CADLGLRVDL YQPMRDIEAV
PAEEFARNLR RARHKFELMR RLGADTVLVC SSVSPLAADD DALAAEHLAR LAGLAEEFGI
RVAYEALAWG RHVDTYDHAW RIVEAAGHPA LGTCLDSFHI LSRGSDPKGI EDIPGEKIFF
LQLADAPLPA MDVLQWSRHH RCFPGQGGFD VAGLVRHVLR TGYTGPLSLE VFNDVFRQAE
AGPTAVDARR SLLVLQEAVG TADLPAPVVP TGIAFAELVT HDTEPVSALL GALGFARTAR
HRTKPVDLWQ QGEARVLVNT GPAVPRGATG LAAVGLRSPR PSAAARRAEA LLAPVLPRRR
APEDAPLDAV AAPDGTELFF CPEPARPAPG EQPGGPAEPP RPDWRADFEP VAHGPAATAV
RRIDHLALTQ PWHHFDEAAL FHRGVLGLHA QESVDVADPY GLLRSRAVTN SDGSVRIALA
VGAAPGDDTG RAQHIALATD DVIAAARRFR AAGGRLLPVP ANYYDDLAAR HDLTEEELRT
YRELGILYDR DPHGVFRHCY TRTVGRVFFE LVQRDGGYRG YGAVNAPVRL AAQHAVRAVT
GG
//