DHQS_ACTCC
ID DHQS_ACTCC Reviewed; 445 AA.
AC U3KRF2; A0A2R6Q234;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 3.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=3-dehydroquinate synthase, chloroplastic;
DE EC=4.2.3.4;
DE Flags: Precursor;
GN Name=DHQS; Synonyms=AROB;
GN ORFNames=CEY00_Acc24429 {ECO:0000312|EMBL:PSS00459.1};
OS Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=1590841;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF
RP 69-445 IN COMPLEX WITH NAD, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=23916589; DOI=10.1016/j.abb.2013.07.022;
RA Mittelstadt G., Negron L., Schofield L.R., Marsh K., Parker E.J.;
RT "Biochemical and structural characterisation of dehydroquinate synthase
RT from the New Zealand kiwifruit Actinidia chinensis.";
RL Arch. Biochem. Biophys. 537:185-191(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Red5;
RX PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT highlights the challenges associated with draft genomes and gene prediction
RT in plants.";
RL BMC Genomics 19:257-257(2018).
CC -!- FUNCTION: Catalyzes the second step in the shikimate pathway.
CC {ECO:0000269|PubMed:23916589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000269|PubMed:23916589};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:23916589};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:23916589};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH
CC 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:23916589};
CC Note=kcat is 20.1 sec(-1).;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:23916589};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:23916589};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23916589}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000305}.
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DR EMBL; NKQK01000021; PSS00459.1; -; Genomic_DNA.
DR PDB; 3ZOK; X-ray; 2.40 A; A/B/C/D=69-445.
DR PDBsum; 3ZOK; -.
DR AlphaFoldDB; U3KRF2; -.
DR SMR; U3KRF2; -.
DR STRING; 1590841.U3KRF2; -.
DR EnsemblPlants; PSS00459; PSS00459; CEY00_Acc24429.
DR Gramene; PSS00459; PSS00459; CEY00_Acc24429.
DR OMA; IKMAVCF; -.
DR SABIO-RK; U3KRF2; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000241394; Chromosome lg21.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IDA:UniProtKB.
DR HAMAP; MF_00110; DHQ_synthase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Chloroplast; Lyase; Metal-binding; NAD; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..445
FT /note="3-dehydroquinate synthase, chloroplastic"
FT /id="PRO_0000425861"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 153..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 186..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 211..212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 251..254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 266
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23916589,
FT ECO:0007744|PDB:3ZOK"
FT BINDING 329
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="H -> P (in Ref. 1)"
FT CONFLICT 24
FT /note="T -> S (in Ref. 1)"
FT CONFLICT 37..43
FT /note="HSLSLRC -> PTLSLRR (in Ref. 1)"
FT CONFLICT 58..60
FT /note="MRA -> LSS (in Ref. 1)"
FT CONFLICT 140
FT /note="G -> E (in Ref. 1)"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:3ZOK"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:3ZOK"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 294..314
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 346..363
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:3ZOK"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:3ZOK"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:3ZOK"
SQ SEQUENCE 445 AA; 48145 MW; F6D8132941A7A829 CRC64;
MAAFSLSAKQ ILSPSTHRPS LSKTTTADSS LRFRNPHSLS LRCSSLSSSS NVGRTRLMRA
SASSTAPVMD TSPTKAVSSA PTIVDVDLGD RSYPIYIGSG LLDQPDLLQR HVHGKRVLVV
TNSTVAPIYL DKVVGALTNG NPNVSVESVI LPDGEKYKNM DTLMKVFDKA IESRLDRRCT
FVALGGGVIG DMCGYAAASF LRGVNFIQIP TTVMAQVDSS VGGKTGINHR LGKNLIGAFY
QPQCVLIDTD TLNTLPDREL ASGLAEVVKY GLIRDANFFE WQEKNMPALM ARDPSALAYA
IKRSCENKAE VVSLDEKESG LRATLNLGHT FGHAIETGFG YGQWLHGEAV AAGMVMAVDM
SYRLGWIDES IVNRAHNILQ QAKLPTAPPE TMTVEMFKSV MAVDKKVADG LLRLILLKGP
LGNCVFTGDY DRKALDETLH AFCKS
