ID E3JWD1_PUCGT Unreviewed; 932 AA.
AC E3JWD1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN ORFNames=PGTG_02797 {ECO:0000313|EMBL:EFP76356.1};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP76356.1, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; DS178265; EFP76356.1; -; Genomic_DNA.
DR RefSeq; XP_003320775.1; XM_003320727.2.
DR AlphaFoldDB; E3JWD1; -.
DR STRING; 418459.E3JWD1; -.
DR EnsemblFungi; EFP76356; EFP76356; PGTG_02797.
DR GeneID; 10534249; -.
DR KEGG; pgr:PGTG_02797; -.
DR VEuPathDB; FungiDB:PGTG_02797; -.
DR eggNOG; KOG0053; Eukaryota.
DR eggNOG; KOG1511; Eukaryota.
DR HOGENOM; CLU_009484_1_0_1; -.
DR InParanoid; E3JWD1; -.
DR OMA; QPYRFST; -.
DR OrthoDB; 6018at2759; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 595..670
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 777..839
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 100877 MW; 307C63DE0FEDC72B CRC64;
MNNNNNNSST LDQSTNSSSD QSSPLSASVV SSSSRVARQP APHRFSTLCA TVENPDQDHQ
DRYGSSSVPI YQSSTFKGVD GLYDYTRSGN PSRTFLQHHV AKISKAKHAF AVSSGMAALD
VILRTLQPGD EIIAGNDLYG GSNRLLTYVK EHNGIITHHI DTTNLENLKP FLVKDSRVRM
VLLESPTNPL LQIVDIEAVI NLVKAVIPEA IIVVDNTMMS PYLMKPLEFG ADVVYDSGTK
YLSGHHDVMA GLVTCNSDKI AKQLAFVINS IGNGLAPFEC FLLTRGIKTL SLRMDRQQAS
AIRVAKYLDQ LGFKVNFPGL AHHKGKEIHD RLAKGPGAVL SFETGDKKLS EKIVSSARLW
SVSVSFGCVN SLISMPCLMS HASIDPAVRA ARNLPEDLIR LCVGIEDPDD LLEELQAALV
EAGAIRILDE TRVDSGYERV GMNSLPISPA EAMIPQKDYL GSSGNPTTLL VSAPGKIILF
GEHAVVYGKK AIAAAVNRRC YCFVEPGGYQ TIETVALCLP DSGWSGSWPI NQLPWDCVKP
TGEGELHVNP QLSQALLTKV AGQADKNSVL QAAHAFLYLF MHLATKENRR SQVFTIRSTL
PIGAGLGSSA SYSVCLASAL LYSHQHIAIP TQKGIETTQV ETINRWAFLG EKILHGSPSG
VDNTVSSFGG AICFQKLIGE NDQQKRQSIE QIQGFGAIRI LISDTQVPRD TKSLVAGVAQ
KKEKDPKLVQ SILDEIEELT ISAQESIKEL AVIKQPDSKD GQNPDQELLK TKRNKILNQL
GHLMARNHSL LSSLGVGHSQ LDLVKSFAAN CGLETKLTGA GGGGCAITLI PDNFEEEKLS
TIVTNIEAHS MKAYETEIGV SGVGILNNLD HHHQLLESVK KIYLTSDLTT LSQSLSNPSQ
ALSRVNPQPD TISNGDSSAP GVPTRDLFWS FA
//
