ID A0A1B0C478_9MUSC Unreviewed; 554 AA.
AC A0A1B0C478;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|RuleBase:RU004164};
DE EC=2.5.1.19 {ECO:0000256|RuleBase:RU004164};
OS Glossina palpalis gambiensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI048659-PA, ECO:0000313|Proteomes:UP000092460};
RN [1] {ECO:0000313|Proteomes:UP000092460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPPI048659-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI048659-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001871};
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|RuleBase:RU004164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001115};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000256|RuleBase:RU004164}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
CC {ECO:0000256|RuleBase:RU004164}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
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DR EMBL; JXJN01025292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0C478; -.
DR STRING; 67801.A0A1B0C478; -.
DR EnsemblMetazoa; GPPI048659-RA; GPPI048659-PA; GPPI048659.
DR VEuPathDB; VectorBase:GPPI048659; -.
DR UniPathway; UPA00053; UER00089.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000092460; Unassembled WGS sequence.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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:0006564; P:L-serine biosynthetic process; IEA:InterPro.
DR CDD; cd02020; CMPK; 1.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR Pfam; PF00275; EPSP_synthase; 2.
DR SUPFAM; SSF55205; EPT/RTPC-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004164};
KW Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU004164};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004164}.
FT DOMAIN 4..320
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 306..377
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 382..451
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 447..552
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000259|Pfam:PF02224"
SQ SEQUENCE 554 AA; 63473 MW; 0791A7AC67A15A51 CRC64;
MKKIFNFSAG PSMLPKTVLI KVKNELFNWN NTNVSIMEIS HRNKKFLNLI ETMKQDLRDL
LYIPKNYNIM FLQGGARTQF SSIPINLINK ISETADYIDS GYWGKYAAYE AKKYCIVNLI
NVIYKEKLKK SVFPMKSWKI SKNSKYVHYC PNETIDGIAI NETPNFTDKL IIGDFSSTLL
SKPIDINKFG IIYASSQKNI GTSGMTVFIF RNDLIFNNNK NIPSCLNYRM LYKYNSLFNT
PPIFNWYVSS LVLKWIKSKG GLLKFNEINQ KKSKLIYKAI DKSNFYYNNI DNLNRSDMNG
NNKALQGFSK IIFLKNSGTA MRFLTAALSV QKNNVILMGN SRMHQRPIGP LVDALRQGGA
KIDYLNKENF PPLKIFGGYR GDSGMTAAII ALFCKNSSIL KNIQNWKFKE CDRINAMLIG
LKKIGAYYFC QGNNLIIYPP KKFIRATIET FYKPPGLVAE GRDMGSIVFP KAYFKIFLDA
SLKIRAERRT KQLQNQGFNV TFKEIFSKIR DRDNSDINRK IAPLIPGKNA LIINSTLLNV
EEVVQIIFDF VKNS
//
