UniProt: R9AM93

Database: UniProt
Entry: R9AM93_WALI9

LinkDB:  R9AM93_WALI9 
Original site:  R9AM93_WALI9

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (12)   
   Pfam (3)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   R9AM93_WALI9            Unreviewed;       893 AA.
AC   R9AM93;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-NOV-2023, entry version 47.
DE   RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE            EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN   ORFNames=J056_004542 {ECO:0000313|EMBL:EOR01221.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR01221.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+);
CC         Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216;
CC         EC=2.7.1.36; Evidence={ECO:0000256|ARBA:ARBA00029310};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17066;
CC         Evidence={ECO:0000256|ARBA:ARBA00029310};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 1/3. {ECO:0000256|ARBA:ARBA00029438}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC       subfamily. {ECO:0000256|ARBA:ARBA00006495}.
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DR   EMBL; KE007231; EOR01221.1; -; Genomic_DNA.
DR   RefSeq; XP_009268012.1; XM_009269737.1.
DR   AlphaFoldDB; R9AM93; -.
DR   STRING; 1299270.R9AM93; -.
DR   GeneID; 20377494; -.
DR   KEGG; wic:J056_004542; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   eggNOG; KOG1511; Eukaryota.
DR   HOGENOM; CLU_009484_1_0_1; -.
DR   OMA; QPYRFST; -.
DR   OrthoDB; 6018at2759; -.
DR   UniPathway; UPA00057; UER00098.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR   GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006238; Cys_b_lyase_euk.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006205; Mev_gal_kin.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01329; cysta_beta_ly_E; 1.
DR   NCBIfam; TIGR00549; mevalon_kin; 1.
DR   PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PRINTS; PR00959; MEVGALKINASE.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lyase {ECO:0000313|EMBL:EOR01221.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          579..665
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          748..801
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
SQ   SEQUENCE   893 AA;  95748 MW;  AD8257B62C670965 CRC64;
     MTDGSSKGPD KYNFSTECVT IDNPDAGKDQ FNSSSVPIYQ SATFKGMNGE YDYSRSGNPT
     RTHLQHHLAK ISSAKHAFAV SSGMAALDVI ARILKPGDHV VAGDDLYGGS NRLLGYLQSN
     AGVVVHHIDT CTPSTVEQYL DKERTRLVLL ETPTNPLIKI CDVQEIASRV KAVCPSAIIV
     VDNTMMSPYL QRPLNFGADV VYDSATKYLS GHHDLMAGVV ICNRDDLAKH MSFTINSVGN
     GLGPFDSFLL LRGLKTLAIR MDRQQASAKI IASFLNQLQF QVHYPGLKNH PGHHTHFKMA
     KDAGAVLSFE TRDIKTSERI VGAAKLWGIS VSFGAVNSLI SMPCLMSHAS IPAHLRAERG
     LPEDLIRLCV GIEDWEDLID DLECSLVQAG AIRRREEQST SSTLSSPEGS LERVGEERAL
     GWQRCLPSDA NNASMDGALQ QPHTSGDAEN IVVSAPGKVI LFGEHAVVHG VTAIASALDL
     RCYGCLGARS DDTIHLVLPD LHSEYSTKVS ALPWAETEVE KSDASDGDGN DVDMNPTLIA
     AIEKTLPPSI TGKIRGAVVA FVHHYMSLCY PTKPSLTFTA RSSIPIGAGL GSSAAYSTCV
     SAALLLYMQK VVINRQRATP HISHSGRKYI GVDIAATVNK WAFASERILH GTPSGIDNSV
     SVFGGAISYA RGRAQPMIPL QGFQSMLLLL ANTHVERDAK AVISRVHALK ANQPGLFDEC
     MRRIQDVVDE AVRCFQDTDL PRESMLVGLG KLVAANHAQL ELLGVSHPAL EMIIAKLKAY
     GLQTKLTGAG GGGCTVTLLP DSFGAGGESG KSGESAHTLA HVTSNLAQNG FSSIVTTVGG
     SGLGVLIDKK VWDMRLVDQD ARESVAPLAG IFTQSSAEEL AGKMKECGHW VFV
//

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