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AROK_METVS
ID   AROK_METVS              Reviewed;         283 AA.
AC   A6URV6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00370};
DE            Short=SK {ECO:0000255|HAMAP-Rule:MF_00370};
DE            EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00370};
GN   Name=aroK {ECO:0000255|HAMAP-Rule:MF_00370}; OrderedLocusNames=Mevan_1331;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00370};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7. {ECO:0000255|HAMAP-Rule:MF_00370}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00370}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Archaeal shikimate
CC       kinase subfamily. {ECO:0000255|HAMAP-Rule:MF_00370}.
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DR   EMBL; CP000742; ABR55228.1; -; Genomic_DNA.
DR   RefSeq; WP_012066143.1; NC_009634.1.
DR   AlphaFoldDB; A6URV6; -.
DR   SMR; A6URV6; -.
DR   STRING; 406327.Mevan_1331; -.
DR   EnsemblBacteria; ABR55228; ABR55228; Mevan_1331.
DR   GeneID; 5325165; -.
DR   KEGG; mvn:Mevan_1331; -.
DR   eggNOG; arCOG01025; Archaea.
DR   HOGENOM; CLU_073768_0_0_2; -.
DR   OMA; WDVLVWT; -.
DR   OrthoDB; 98200at2157; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000001107; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid 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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00370; Shik_kinase_arch; 1.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR010189; SK_arc.
DR   PANTHER; PTHR20861:SF3; PTHR20861:SF3; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF005758; Shikimt_kin_arch; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR01920; Shik_kin_archae; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..283
FT                   /note="Shikimate kinase"
FT                   /id="PRO_1000059939"
FT   BINDING         86..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00370"
SQ   SEQUENCE   283 AA;  30579 MW;  182444E17511439C CRC64;
     MRCSAISPGS GTIINAISTG KGSAFGIDLK IKANVELKND GKSKINGILL DNPSLKPNLV
     ERCVKNVLEH FEVDYSAKIS TSSELPLKSG LSSSSAASNA AVLATFGALG EKIDSELILD
     LAIKSSFEEQ LTITGAYDDA TASYFGGITV CNNLERKILK KDVFKEELDV IILMPNFKKN
     LNVKRMKLIS DYVELAFEKC MNADYYKALF LNGILYSSAL NFPSYISVDA LEAGAVTAGL
     SGTGPSYIAL SYQENTEKVK NAFKKYGTVI ISKPDNFGSK IIY
 
 
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