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Database: UniProt
Entry: A0A0M8VIV7_9ACTN
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Original site: A0A0M8VIV7_9ACTN 
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
//
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