ID A0A2K8PBY0_STRLA Unreviewed; 271 AA.
AC A0A2K8PBY0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ATZ24239.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:ATZ24239.1};
GN Name=thiD {ECO:0000313|EMBL:ATZ24239.1};
GN ORFNames=SLAV_11875 {ECO:0000313|EMBL:ATZ24239.1}, SLLC_09925
GN {ECO:0000313|EMBL:QUQ54070.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ24239.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ24239.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ24239.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ54070.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ54070.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000256|ARBA:ARBA00003848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000565};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3. {ECO:0000256|ARBA:ARBA00004769}.
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DR EMBL; CP024985; ATZ24239.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ54070.1; -; Genomic_DNA.
DR RefSeq; WP_037686630.1; NZ_JOEW01000006.1.
DR AlphaFoldDB; A0A2K8PBY0; -.
DR GeneID; 82164372; -.
DR KEGG; slx:SLAV_11875; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; Chromosome.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ATZ24239.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231791};
KW Transferase {ECO:0000313|EMBL:ATZ24239.1}.
FT DOMAIN 20..265
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 271 AA; 27459 MW; 0160EFC395BDE3EB CRC64;
MTRQAPHPHP PLCLTVAGSD SGGGAGIQAD LKTMLALGVH GMSVVTAVTA QNSLGVRGAW
ELPAQAVTAQ YRAVVDDIGV QAVKTGMLSS AVLVETVAGL LAGTAAPVVV DPVGVSKHGD
ALLAASALDA VRRELLPRAT VATPNLDEVA QLTGLTVTDE DGMRRAADAV LGHGPRWALI
KGGHLAAHGG EAVDLLTDGS EELWLRAPRY DNRHTHGTGC TLASAVAAGL AKGLAVPEAV
TAAKEYVTGA IAAGFALGAG IGPVDHAWQW R
//
