ID A0A0A1CWV7_9MICC Unreviewed; 529 AA.
AC A0A0A1CWV7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase multifunctional protein {ECO:0000313|EMBL:AIY00644.1};
DE EC=2.5.1.3 {ECO:0000313|EMBL:AIY00644.1};
GN ORFNames=ART_1045 {ECO:0000313|EMBL:AIY00644.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY00644.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY00644.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY00644.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) 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; CP007595; AIY00644.1; -; Genomic_DNA.
DR RefSeq; WP_052136012.1; NZ_CP007595.1.
DR AlphaFoldDB; A0A0A1CWV7; -.
DR STRING; 1494608.ART_1045; -.
DR KEGG; arm:ART_1045; -.
DR HOGENOM; CLU_020520_2_1_11; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000030301; 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:AIY00644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030301};
KW Transferase {ECO:0000313|EMBL:AIY00644.1}.
FT DOMAIN 33..280
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 316..509
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 55535 MW; ECA4E4FD3035DF90 CRC64;
MSATTLFSPA HEATGTAQSP WKHPRVLSIA GSDPSGGAGI QADIKSISAH GGYAMAAITA
LTAQNTRGVQ GVHVPPAEFL RSQLDALASD ITIDAVKIGM LGTAEVMNTV GEWLAHTRPS
AVVLDPVMVA TSGDTLMAPE ALEALLALLA NTHLVTPNIP ELAALLGQSE VGSWAEAVQQ
GRELAAAHNV MVLVKGGHLP GEQCLDALVG VDGAIQEFTA PRIHTANTHG TGCSLSAAVA
TLQARTGDWG QAVGTAKAWL VGALEASEVL DVGAGAGPIH HLHALWATAA PSLDAFSRVL
WQDCAPQRQA IFGLDFIKEL AAGTLARDRF AYYLAQDALY LATYSRVLAR ASALAPTEAE
QKFWAGGAQN ALDVELALHR DWLSHYPLDS PEGPEQEGPE LGPVTKHYVD HLQGVAFSGS
YGEVVAAVLP CYWLYAEVGR VLHADYLARA GGHPYGTWLQ TYADDDFAQA TATAVGIMDA
AARNGSAAER TRMRRAFAHS AQYEVDFFAA PHQQFAGPGG GVTPSNVSW
//
