ID H3GHV1_PHYRM Unreviewed; 1547 AA.
AC H3GHV1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|PIRNR:PIRNR000514};
DE Includes:
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|PIRNR:PIRNR000514};
DE Short=DHQS {ECO:0000256|PIRNR:PIRNR000514};
DE EC=4.2.3.4 {ECO:0000256|PIRNR:PIRNR000514};
DE Includes:
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|PIRNR:PIRNR000514};
DE EC=2.5.1.19 {ECO:0000256|PIRNR:PIRNR000514};
DE Includes:
DE RecName: Full=Shikimate kinase {ECO:0000256|PIRNR:PIRNR000514};
DE Short=SK {ECO:0000256|PIRNR:PIRNR000514};
DE EC=2.7.1.71 {ECO:0000256|PIRNR:PIRNR000514};
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|PIRNR:PIRNR000514};
DE Short=3-dehydroquinase {ECO:0000256|PIRNR:PIRNR000514};
DE EC=4.2.1.10 {ECO:0000256|PIRNR:PIRNR000514};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase {ECO:0000256|PIRNR:PIRNR000514};
DE EC=1.1.1.25 {ECO:0000256|PIRNR:PIRNR000514};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra75561, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra75561}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra75561};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC reactions in prechorismate polyaromatic amino acid biosynthesis.
CC {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10;
CC Evidence={ECO:0000256|PIRNR:PIRNR000514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00001901,
CC ECO:0000256|PIRNR:PIRNR000514};
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:0000256|PIRNR:PIRNR000514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC EC=2.7.1.71; Evidence={ECO:0000256|PIRNR:PIRNR000514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000256|PIRNR:PIRNR000514};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR000514};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRNR:PIRNR000514};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
CC {ECO:0000256|ARBA:ARBA00009948}.
CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000256|ARBA:ARBA00006477}.
CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the dehydroquinate
CC synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC family. {ECO:0000256|ARBA:ARBA00009349}.
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DR EMBL; DS566010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 164328.H3GHV1; -.
DR EnsemblProtists; Phyra75561; Phyra75561; Phyra75561.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_1_2_1; -.
DR InParanoid; H3GHV1; -.
DR OMA; SWANMSW; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00502; DHQase_I; 1.
DR CDD; cd08195; DHQS; 1.
DR CDD; cd01556; EPSP_synthase; 1.
DR CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR HAMAP; MF_03143; Pentafunct_AroM; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008289; Pentafunct_AroM.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR NCBIfam; TIGR01356; aroA; 1.
DR NCBIfam; TIGR01357; aroB; 1.
DR NCBIfam; TIGR01093; aroD; 1.
DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR000514};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|PIRNR:PIRNR000514};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000514};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000514};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR000514};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000514};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000514};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000514};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000514}.
FT DOMAIN 78..336
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT DOMAIN 379..803
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 1259..1343
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 1382..1456
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 1547 AA; 167786 MW; D72E5013C3470CEC CRC64;
MSAPQVVSCG SYDIVLGSSL LQSRFVAEDL LQRLPSTATF VILTDANVGP LYAEPLRVQL
AALLHAQGNT TRRVLLHAIP SGEASKCREM KAKIEDEVLF PNRCHRDTCI VAVGGGVVGD
LSGYVASTYM RGVPFVQVPT SLLACVDSSI GGKTGIDVEA GKNLLGAFHM PQRVYIDLSV
LHTLPKRELI NGMGEVVKSG AIFNAELFEL LETSAESILA LSDMDLVQRV VALTVQVKAT
VVTQDTKEMG LRAILNFGHS IGHGIEALVQ PEYLHGECVS MGCIKEAEIA RGMGVCSSAT
VGRLRRCLAS YGLPVRVPEH VATRDVLVKM EVDKKNSQGV KKIVLLEKIG KVLADPYARA
VKDHQIELVL EKQVRMVPGA KANGTIRVPG SKSISNRVLL MAALGKGACR ITGLLHSDDT
QVMMTALQKV GAKFSWEDNG AVLVVEGTAG KFATVADGEE IYLSNAGTAA RFLTSAMTLV
PSENDGTVVV TGNYRMKERP IAPLVEALRG NGCDISYLET EGCPPLAIRG TGLRGGTVRL
AAKVSSQYVS SVLISAPYAK EPLVLELDEE QPTSLPYILM TTQLMQQFGI PVETLAPNRY
RVPCGVYENP KEVSVEVDAS SATYPLAFAA ITGGQVTVEA LGNTSLQGDA AFHTLLRSMG
CTTTQDATST TVIGPQDGTP LKAVDIDMET MTDAFMTAVA LAAVADGTTK ITGIANQRVK
ECNRIEVMVT ELHKIGVECG ELPDGIWIKG TAGKTDHLKQ ASIACHNDHR IAMSFAVLGS
VVGNVVITDK ECTDKTYPEF WDHVQMHLGL QVAPVVEETT DSNDSDTSIP GVFMIGMRGA
GKSSLAKAAS ATLKLNLLDT DKVLEKEFGE SIADFVARHN HTWEAFREKQ KELLLRLIAN
PPPATIISCG GGVVETPEIV AALEKYPYVV HVHRDIRDVL AYLDTVEESH RPSLGDSHAN
VWARREPLYQ RSATFEFVVT AGDVDYPRLD RDFVRFLSVI TPGLPTNFDY RSSCRADTFF
LSLTFPDMND ARPIISDISK GADALELRVD LLKYPQDTKF VAAQVALLRT LSSLPIIFTV
RSKGQGGAFP DGEENELKMF ELLQLGVRLG CEFVDMETCW SRKAREHLLA HRYRSAIISS
FHAVQKPTSE AETKLIFREC YSQGRVQIVK VVVKAYSPQD ALMVDRVAKD FANAWQQQMP
IISLCTTEAG KLTRVLNRTL TPVTHPLLPA AAAPGQLSIE EIMILRKQLG LLPAREFFLF
GSPIQKSPSP AMHNAGFEST SLSSLFTYGL HDTTDVLEIV KRMQAPDTCF GGGSVTIPLK
VDIMAHLNEL SPAARAIGAV NTIMREDRNG SPYWKGDNTD WLGILRPISK RLATLSVRKP
AHELTALVVG AGGTSMAASY AMRQLGVGKL FIFNRTLEKA QAVAARFDAE ALSELTPETL
AQVDVVVGTI PAQAGFQLPD HLVAPRADGS KVVVLDAAYM PPITPMLAHA HASGGALCIQ
GYEMLYEQGI EQFYRWHKAT QVWVVNEEAI KEACRQHVPI DQRLSQA
//
