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Database: UniProt
Entry: A0A1M5UKN8_9EURY
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ID   A0A1M5UKN8_9EURY        Unreviewed;       291 AA.
AC   A0A1M5UKN8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN05443636_3054 {ECO:0000313|EMBL:SHH63584.1};
OS   Halobaculum gomorrense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halobaculum.
OX   NCBI_TaxID=43928 {ECO:0000313|EMBL:SHH63584.1, ECO:0000313|Proteomes:UP000184357};
RN   [1] {ECO:0000313|EMBL:SHH63584.1, ECO:0000313|Proteomes:UP000184357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9297 {ECO:0000313|EMBL:SHH63584.1,
RC   ECO:0000313|Proteomes:UP000184357};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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: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}.
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DR   EMBL; FQWV01000011; SHH63584.1; -; Genomic_DNA.
DR   RefSeq; WP_073311137.1; NZ_FQWV01000011.1.
DR   AlphaFoldDB; A0A1M5UKN8; -.
DR   STRING; 43928.SAMN05443636_3054; -.
DR   OrthoDB; 9602at2157; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000184357; 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; IPR013750; GHMP_kinase_C_dom.
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; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF005758; Shikimt_kin_arch; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00370};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00370};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00370};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00370};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00370, ECO:0000313|EMBL:SHH63584.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00370};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184357};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00370}.
FT   DOMAIN          78..154
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          227..273
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   BINDING         85..95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00370"
SQ   SEQUENCE   291 AA;  29344 MW;  5AAC8D250A490AA9 CRC64;
     MEGRAAAPGA GTVVNALATG RGAAFALDLE TTATVRLDPD ADGVSGTIAG APDGDTTLIE
     RCVERVVDRY GADEGGTVET DSEVPTAAGL KSSSAAANAT VVATLSALGL EVANDPDADV
     TKTEACRVGV RAARDAGVTV TGAFDDASAS MLGGVTVTDN REDDLLASGD PFAEHALVWT
     PLERAYSADA DVGACERVAP MAELATELAL NGDYARAMTV NGLAFSAALG FPSDPAVEAM
     ADCAGVSLSG TGPSVVAVGD RDALAAVRER WAARDGETRL TRTRETGARV L
//
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