ID I3D1T6_9ARCH Unreviewed; 284 AA.
AC I3D1T6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=BD31_I1737 {ECO:0000313|EMBL:EIJ65679.1};
OS Candidatus Nitrosopumilus salaria BD31.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=859350 {ECO:0000313|EMBL:EIJ65679.1, ECO:0000313|Proteomes:UP000003423};
RN [1] {ECO:0000313|EMBL:EIJ65679.1, ECO:0000313|Proteomes:UP000003423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD31 {ECO:0000313|EMBL:EIJ65679.1,
RC ECO:0000313|Proteomes:UP000003423};
RX PubMed=22461555; DOI=10.1128/JB.00013-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome sequence of "Candidatus Nitrosopumilus salaria" BD31, an ammonia-
RT oxidizing archaeon from the San Francisco Bay estuary.";
RL J. Bacteriol. 194:2121-2122(2012).
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:EIJ65679.1}.
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DR EMBL; AEXL02000105; EIJ65679.1; -; Genomic_DNA.
DR RefSeq; WP_008299961.1; NZ_AEXL02000105.1.
DR AlphaFoldDB; I3D1T6; -.
DR PATRIC; fig|859350.6.peg.1275; -.
DR OrthoDB; 9602at2157; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000003423; 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 Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 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 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:EIJ65679.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00370};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00370, ECO:0000313|EMBL:EIJ65679.1}.
FT DOMAIN 78..146
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT BINDING 85..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00370"
SQ SEQUENCE 284 AA; 30382 MW; 89BF3E57CFABD77A CRC64;
MAKAKATVHG AISLVNAIAN QKGATLGIAL KVEATVETSP GKGIIIQSEN KSLSSRLINK
TVEKIISKKD LEQNKITITL ESEIPTGYGL KSSSAISSAV ALACTKIFKP KFTDQQILLA
GVEASIESKV SITGAYDDAC SCYYGGFNVT DNAKKKRIRF EKGPSDLVAV IFIPKNRKRG
NLKKLKILSP VFEIAWELAR KANYWEAMTV NGLATASILN SDPKIITDLI EKGALAASVS
GNGPSIAAVV KKENESTIKK IFSTLEGNVI VSRISNEKAK VNEV
//
