ID A0A0G4KXU0_9PEZI Unreviewed; 1274 AA.
AC A0A0G4KXU0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|RuleBase:RU004164};
DE EC=2.5.1.19 {ECO:0000256|RuleBase:RU004164};
GN ORFNames=BN1708_017263 {ECO:0000313|EMBL:CRK14511.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK14511.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK14511.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK14511.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004164};
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|ARBA:ARBA00000172};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000256|ARBA:ARBA00004842}.
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|RuleBase:RU004164}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
CC {ECO:0000256|ARBA:ARBA00009948, ECO:0000256|RuleBase:RU004164}.
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DR EMBL; CVQH01005559; CRK14511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4KXU0; -.
DR STRING; 100787.A0A0G4KXU0; -.
DR OrthoDB; 865at2759; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
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:InterPro.
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-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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_00109; Shikimate_kinase; 1.
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; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR010110; Shikimate_DH_AroM-type.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR NCBIfam; TIGR01356; aroA; 1.
DR NCBIfam; TIGR01357; aroB; 1.
DR NCBIfam; TIGR01809; Shik-DH-AROM; 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; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 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; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU004164};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU004164};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004164};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 79..358
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT DOMAIN 402..831
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 989..1062
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
SQ SEQUENCE 1274 AA; 136300 MW; 29D3C4AC5148FD23 CRC64;
MSSSNTTEPT RIPILGTDNI VVDHGIWLNW VTKDLFDNVK SSTYVLVTDT NLYDTYVPPF
KHAFYGAADT TARPRLLTLA IPPGEISKSR QSKAHIEDWM LSQQCTRDTV IIALGGGVIG
DMLGYVAATF MRGIRFVQVP TTLLAMVDSS IGGKTAIDTP MGKNLVGAFW QPSRIYIDLA
FLETLPSREF INGMAEVIKT AAIWDENEFT ALEANAPSIV AAVNQPTGPG RLSPIRDILK
RIVLGSARVK AEVVSSDERE GGLRNLLNFG HSIGHAYEAL LTPQLLHGEA VAIGMVKEAE
LARYLGVLRP SAVARLAKCI SSYGLPTSLG DKRVIKLTAG KRCPVDILLQ KMAVDKKNDG
RKKKIVLLSA IGKTHEPRAT TVKDAAIKVM LSASTLVTPG VPTKLATTVT PPGSKSISNR
ALILAALGEG TCRIKNLLHS DDVEFMLTAI TRLGGASYAW EDAGEVLVLT GKGGQLRASS
DPLYLGNAGT ASRFLTTVVA LCSPADVSST VLTGNARMQV RPIGPLVDAL RSNGVSIDYL
GPGKSLPLRI DAAGGFAGGV IELAATVSSQ YVSSILMAAP YAKEPVTLRL VGGKPISQPY
IDMTLAMMKT FGVQAERSSS DPNTYHIPKG TYKNPAEYTI ESDASSATYP LAIAAITGTT
CTVPNIGSSS LQGDARFAID VLQPMGCTVQ QTATSTTVTG PAPGGLLGLP HVDMEPMTDA
FLTASVLAAV AAGTTKISGI ANQRVKECNR IAAMREQLGK FGIATDEFDD GIIVTGQPLD
TLKTPDAGVF CYDDHRVAMS FSVLSTVANA PVTILERECT GKTWPGWWDT LSQSFGLRLN
GDDKHPGAEG HHQQDHTTRS VFIVGMRGAG KTTTGRWMAK LLKRPFIDLD EELERRSGMT
IPEMIHGTKG WEGFRRDELQ LLHDVMENQA TGHVFSCGGG ILSRVLNGFL TPVSHPALPF
KAAPGQLSAA EIRRALFLLG NIDAQSFYLF GKPISKSRSP ALHNSLFDLT GLPHKYGLVE
TDQADEVAAV GASVTIPLKL DVMPLLDEVS ESAKVIGAVN TIIPIPLDGS QKRRLLGDNT
DWRGMVHCLE SIGVASESTA GTTTASALVI GSGGTTRAAI FALKSYGYHP IYMLARNEQS
LETIRASFPA DFDLRALRGP AEASTLAVAP TVVISTIPAD KPMDPSLRET LEVVLRSPVS
EQRTRVLLEM AYQPRHTAAM RLAEDAGWRT IPGAEVLAAQ GWHQFQMWTD ITPRFIDAQA
AVNGDVLPTS TDQP
//
