ID V1CNQ6_9FIRM Unreviewed; 915 AA.
AC V1CNQ6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109};
DE Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109};
GN Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN ORFNames=HMPREF9089_00785 {ECO:0000313|EMBL:ESE30501.1};
OS Eubacterium brachy ATCC 33089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=1321814 {ECO:0000313|EMBL:ESE30501.1, ECO:0000313|Proteomes:UP000017536};
RN [1] {ECO:0000313|EMBL:ESE30501.1, ECO:0000313|Proteomes:UP000017536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33089 {ECO:0000313|EMBL:ESE30501.1,
RC ECO:0000313|Proteomes:UP000017536};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000256|HAMAP-
CC Rule:MF_00109}.
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|HAMAP-Rule:MF_00109};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00109};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00109};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00109}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESE30501.1}.
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DR EMBL; AXUD01000006; ESE30501.1; -; Genomic_DNA.
DR AlphaFoldDB; V1CNQ6; -.
DR STRING; 1321814.HMPREF9089_00785; -.
DR PATRIC; fig|1321814.3.peg.745; -.
DR eggNOG; COG0082; Bacteria.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_318019_0_0_9; -.
DR OrthoDB; 9771806at2; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000017536; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProt.
DR GO; GO:0004107; F:chorismate synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
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-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR CDD; cd00464; SK; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.60.150.10; Chorismate synthase AroC; 1.
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_00109; Shikimate_kinase; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR NCBIfam; TIGR00033; aroC; 1.
DR PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00109};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00109};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022643};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000313|EMBL:ESE30501.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW Reference proteome {ECO:0000313|Proteomes:UP000017536};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00109}.
FT DOMAIN 389..470
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT BINDING 753..758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 757
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 775
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 799
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 828
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 876
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ SEQUENCE 915 AA; 100959 MW; E4FFDC7424A187BD CRC64;
MIRSSFGKNI HIDISGGSHE KSIFVEIWGL PANLKISMES VRGILDERRS KSDGISTTRV
EDDLPLVWSP LTGKYVSVSN IHTAENFPII AKFNNNNFNS AEYDSDFPRL GHCDLPAKMK
YGNEVNLSGG GPFSGRMTVA LCFAGAVAME ILKSKGIDIG GQVLSVGNEK NTPISLENPH
SSPISDIMIS EAAKAKSDDD SVGGTLEVFA KGLPLGLGGP LFDNLESEIS SCVFSIPAVK
GIEFGAGFKS SQMTGSKFND PILRIEPTDH LGYKMVTSKN DSGGILGGLS TGMPLTLRVA
IKPTPTISSP QKTIDFKTGK NIEHTFHGRH DACIVPRALP CVKSALALCL LDKLIERDLY
HKTHEVLPEG SPGRVVGDLP KWLKPSKNKY AFMDLSSLRS EVLATDQKIQ NLLEERLILT
DLIGEIKKES SLGIFDEDRE RTVLSHLDIK WHDVFRHIMT ISRAEQTNCN KELFGLVGSH
LSHSYSKKIH ESFGEYKYHL IEVDSENFEK FIMDADFTGL NLTFPYKEAV MAYLHPTSVA
KKIGAANTVF FNSRGKLIGT NTDYDGFCHL VNIHGVKLSG KKILILGNGG AGKAVQHAVL
SYSPRSVAVA TRQNLNEIEK IKKISYMNYG DLTDEYDVII NATILGNSPD VNRSPVNLKD
FDKCKTAIDI IYNPFMTEFL LRGKLLGKKV VGGLTMLVGQ AISASNYFIA SAEGIDFSKE
LAFPDFLLEN MIKCSVANIL HDTLDIVIVG MSGAGKTTIG RELAKRLNMP FIDIDEEIEK
ISEKSIREYF AAGEEDSFRK LEAAAVDKIF SIADNLSSKI PRVIATGGGT ISSMENIKLI
SKNSLIIYLD RDLNLIKAKD NPIYENISKR KLYDMRNPIY SEISHIHIKH KNSVKSTLNK
IVSEVESYYE KDYFN
//
