ID A0A1Q7MHT5_9CREN Unreviewed; 290 AA.
AC A0A1Q7MHT5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Shikimate kinase {ECO:0000256|ARBA:ARBA00013853, ECO:0000256|HAMAP-Rule:MF_00370};
DE Short=SK {ECO:0000256|HAMAP-Rule:MF_00370};
DE EC=2.7.1.71 {ECO:0000256|ARBA:ARBA00012154, ECO:0000256|HAMAP-Rule:MF_00370};
GN Name=aroK {ECO:0000256|HAMAP-Rule:MF_00370};
GN ORFNames=AUI97_07605 {ECO:0000313|EMBL:OLD12234.1};
OS Crenarchaeota archaeon 13_1_40CM_3_52_17.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805096 {ECO:0000313|EMBL:OLD12234.1, ECO:0000313|Proteomes:UP000185971};
RN [1] {ECO:0000313|EMBL:OLD12234.1, ECO:0000313|Proteomes:UP000185971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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 ECO:0000256|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:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_00370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00370}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Archaeal shikimate
CC kinase subfamily. {ECO:0000256|ARBA:ARBA00010202, ECO:0000256|HAMAP-
CC Rule:MF_00370}.
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:OLD12234.1}.
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DR EMBL; MNGN01000053; OLD12234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7MHT5; -.
DR STRING; 1805096.AUI97_07605; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000185971; 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: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 Gene3D; 3.30.230.10; -; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR010189; SK_arc.
DR NCBIfam; TIGR01920; Shik_kin_archae; 1.
DR PANTHER; PTHR20861; HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE; 1.
DR PANTHER; PTHR20861:SF3; SHIKIMATE KINASE; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF005758; Shikimt_kin_arch; 1.
DR PRINTS; PR00958; HOMSERKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00370};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00370};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00370}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00370};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00370, ECO:0000313|EMBL:OLD12234.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00370}; Transferase {ECO:0000256|HAMAP-Rule:MF_00370}.
FT DOMAIN 82..150
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT BINDING 89..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00370"
SQ SEQUENCE 290 AA; 30471 MW; 8BDDD7CE18B5C299 CRC64;
MKGTGQALSH GAISILNAFP TGKGGALGVD LWTRAKATLR EGPGQISGLI SSDPQESNNL
IVTVVKKTLE HYGYERKLHG EVITSSNIPT AVGLKSSSAA ANAAALATIS ALGEEQDDEA
LVQIGIEASI ESGVSLTGAY DDSFASYHGG AVLTDNDRRK AEKILKVPRD IRILILVPPR
KTRTGQLDRT RFAPIRRISE LAYSEAGNGH LWDAITLNGL AVSSILGEDP RPALSAIEAG
ALGAGLSGKG PAVTAIVDEN SLKPVRQVFE KFDGQIIEAN PNFTKALIET
//
