ID A0A067CJ36_SAPPC Unreviewed; 1501 AA.
AC A0A067CJ36;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 56.
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};
GN ORFNames=SPRG_08112 {ECO:0000313|EMBL:KDO26822.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO26822.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO26822.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO26822.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583221; KDO26822.1; -; Genomic_DNA.
DR RefSeq; XP_012202470.1; XM_012347080.1.
DR STRING; 695850.A0A067CJ36; -.
DR EnsemblProtists; KDO26822; KDO26822; SPRG_08112.
DR GeneID; 24130349; -.
DR KEGG; spar:SPRG_08112; -.
DR VEuPathDB; FungiDB:SPRG_08112; -.
DR OMA; SWANMSW; -.
DR OrthoDB; 865at2759; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000030745; 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; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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_00110; DHQ_synthase; 1.
DR HAMAP; MF_00210; EPSP_synth; 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; IPR041121; SDH_C.
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 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; PF18317; SDH_C; 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:UP000030745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000514};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000514}.
FT DOMAIN 66..323
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT DOMAIN 363..785
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 1236..1316
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 1340..1395
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 1458..1484
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
SQ SEQUENCE 1501 AA; 159738 MW; 42E7E5E0461C6941 CRC64;
MSSSTKEIPC KDYIVQVGHG LLASVPAQLK TLLPKVGSYM VISDSNVAPL YAKTLLAGFT
DRVELYVIPA GEASKCRRMK QTIEDYMLAK RFHRDCCVVA LGGGVVGDLA GYVAATYMRG
VPFVQIPTSL LACVDSSIGG KTGIDVEAGK NLIGAFHQPK RVFVDLSLLA TLPKRELING
MAEIIKAGAI YSEPLFSLLE TNVDAILSLQ KDVVLDVVAQ SIAVKTTVVN LDVSEQGIRA
ILNFGHSIGH GIEAIMQPEL LHGECVAIGM VKEAEIARGM GLCSSATVGR LLRCIKAFGL
PVRVPARSPS HVVLTNMEVD KKNSGALKKL VLLTSIGAVH SNPYTVAVDD ARILHVLEPQ
VMVQPTGPLQ GSVHVPGSKS ISNRVLLLAA LGRGTCRISG LLHSDDTQVM MDVLQYLGCG
FAWEDDGNVL VVHGTGGVFP KTIPSHWYLS NAGTAARFLT SVATFCGAEI TLTGNHRMQE
RPIADLVDAL NANGCKITYE KTVGCPPLRI QPTGLPGGSM RMQGKVSSQY VSSVLLSAPY
ASAPLDLLLE EDAPTSLPYI LMTTQLMADF GVHVQQTGAN RFSVPRGVYT NPATYHVEVD
ASSATYPLAL AAITGGRVTV PGLGSTSTQG DAAVHTVLRA MGCTTGQDAH STWVQGPAFG
TLTAVNVDMM TMTDAFMTVA VVAAAANGKT TITGIANQRV KECNRIQVMV TELAKCGVLC
GELPDGLWIQ GLGAKAPHFP QTLAKIACHN DHRIAMSFAV LGAVWPHIVI TDKECTDKTF
PSFWDECASS LAMSLTSPTS GRTSSTTSAL PRYVFLVGMR GAGKTSLGKS AALTFGLDWI
DMDDYLEKNV FQTTVKDYVA VHGWDAFRAA EVACLETWMT SAPSSSGPTT IISCGGGLVE
SPAAVGMLQA YPLVVHVERA IADIVAYLET DAARPAYGES VLDVWTRRQP LFAAASQYHF
TVSAGDVDFA RISADFGRFL AVVLRRFDVA KLTRIPDSYF LSLTSPNLHA VTKAELDVLA
TGVHALELRV DLLASTEPAF VADQVARLRS LSPLPIIYTV RSLNQGGAYP DAPGPIFDLL
RLGLRLGCEV VDMECCWESA LQASLLEAKG GSAVLASYHA IQERSTKEKT AELFDLCAWQ
GQVDIAKVVL KAYDISDAYM IHQVLAECKA RWPFHMPTIA VCTTPSGSLS RVLNRTLTPV
THPALPAAAA PGQLSVAEIE TLRKTLGMTP GLSFYLFGSP IAHSPSPAMH NAAFAALQLP
HTYALFESTD ISVYKRVLND PNFGGASVTI PHKVDIIPYL QKLSPAASAI GAVNTLVPNP
VTKSMEGDNT DWLGIYRPIA RRLSPTANGG NALVIGAGGT AMAACYAMQQ LGLHVFVYNR
TLAKATEVAA RFQSTALPTL EAAPTMHVVV GTIPASAGFT LPPALLHKAL IVMDAAYKPA
ITPMLAHASR HGCVCIQGYE MLVEQGLEQS KRWTGASVPI DVLATVVKAR LDPTEILPGG
L
//
