ID A0A2S7U5D8_9BACT Unreviewed; 273 AA.
AC A0A2S7U5D8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:PQJ29393.1};
GN ORFNames=BSZ32_13460 {ECO:0000313|EMBL:PQJ29393.1};
OS Rubritalea profundi.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Rubritaleaceae; Rubritalea.
OX NCBI_TaxID=1658618 {ECO:0000313|EMBL:PQJ29393.1, ECO:0000313|Proteomes:UP000239907};
RN [1] {ECO:0000313|EMBL:PQJ29393.1, ECO:0000313|Proteomes:UP000239907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-165 {ECO:0000313|EMBL:PQJ29393.1,
RC ECO:0000313|Proteomes:UP000239907};
RA Song J., Yoshizawa S., Kogure K.;
RT "Study of bacterial adaptation to deep sea.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PQJ29393.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MQWA01000001; PQJ29393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7U5D8; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000239907; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
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:PQJ29393.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239907};
KW Transferase {ECO:0000313|EMBL:PQJ29393.1}.
FT DOMAIN 14..252
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 273 AA; 29254 MW; DBC4FB7B594E3F45 CRC64;
MYKPQVVLSI AGSDCSSGAG IQADLKAFSY YGTHGLTAIT CVVAETPNQV VSIHPIPPAI
LQDQIRILLE TYQIKAIKTG MLYSKLHIVA ITELLQQQPI PIIVDPVMVA SSGAHLLKDD
AVEAYISRLL PIAQLVTPNL AEASVILNQE ITQVDQLEAA AQEISSIYNI SCLVKGGHLP
AENNRVDVLW HEGKAYRYSA PTVDIESTHG TGCTLSAAIT ANIARGLSIP DAVQVAKDWV
HSAISQSFSF KSADDVPVQA LNQLRPGALK LDL
//
