ID E1VRP6_GLUAR Unreviewed; 474 AA.
AC E1VRP6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:CBT74299.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:CBT74299.1};
GN Name=thiD {ECO:0000313|EMBL:CBT74299.1};
GN OrderedLocusNames=AARI_00570 {ECO:0000313|EMBL:CBT74299.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT74299.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) 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; FQ311875; CBT74299.1; -; Genomic_DNA.
DR RefSeq; WP_013347453.1; NC_014550.1.
DR AlphaFoldDB; E1VRP6; -.
DR STRING; 861360.AARI_00570; -.
DR KEGG; aai:AARI_00570; -.
DR eggNOG; COG0351; Bacteria.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_020520_2_1_11; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000006878; 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 CDD; cd19365; TenA_C-like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
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 Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CBT74299.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006878};
KW Transferase {ECO:0000313|EMBL:CBT74299.1}.
FT DOMAIN 10..254
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 270..464
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 474 AA; 51327 MW; 2B60C948E314CB50 CRC64;
MNILSIAGSD PSGGAGIQAD LKAIAANGGY GMCVITALTA QNTHGVSGVQ AISGDFVLTQ
LEAVSTDIRI DAIKIGMLAN AEVIRAVTSW LETVDAPVVL DPVMVATSGD RLLDDESALD
SLLDRATVIT PNLLELASLL REPVAPSWDE ALRQAQRLAA KHDTLVLAKG GHLAGADCPD
ALVSAGGVQL ELHGARHATR NTHGTGCTLS STLATRFAAT GDWIAALEQS KSYLSKAIAA
ADQLQVGSGH GPVNHFIDFF GTADPMGDWW QKIQPIREEI DQLDFITRLS EGTLDREDFH
YYIAQDALYL LRYAKVLSLA SSMAPDLGAQ RFWSRGANGI LDGELQLHGS YLDEFADTPS
AITLNYTNHL AASQESYGEL IAAILPCYWL YQDIGKRLAA ANHAEHPYRQ WLETYASEEF
DSATEQAIEM VRQAFEQADP QLRARMEAAF IRSAEHERSF FAQAHENRVD FSTA
//
