ID A0A291GL50_9MICO Unreviewed; 560 AA.
AC A0A291GL50;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ATG50951.1};
GN Name=thiD {ECO:0000313|EMBL:ATG50951.1};
GN ORFNames=CFK38_04950 {ECO:0000313|EMBL:ATG50951.1};
OS Brachybacterium vulturis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2017484 {ECO:0000313|EMBL:ATG50951.1, ECO:0000313|Proteomes:UP000218165};
RN [1] {ECO:0000313|Proteomes:UP000218165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM2412 {ECO:0000313|Proteomes:UP000218165};
RA Tak E.J., Bae J.-W.;
RT "Brachybacterium sp. VM2412.";
RL Submitted (SEP-2017) 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; CP023563; ATG50951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GL50; -.
DR KEGG; brz:CFK38_04950; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000218165; 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:ATG50951.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218165};
KW Transferase {ECO:0000313|EMBL:ATG50951.1}.
FT DOMAIN 30..277
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 357..543
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 560 AA; 58028 MW; 08BD27A77C97A7C3 CRC64;
MSPDPCTQSP SALLPARPTV PRVVSIAGTD PTGGAGTAAD LKSITAAGGY GMAVVTAVVA
QNTHGVCDIH VPPAEFLAAQ LTAVSDDVTL EAVKTGMLGT VEVIEAVAAW IDAHPPRVLV
VDPVMVATSG HRLLEPAAER AMLRFCRRAS VVTPNIDELA VLTGAPRART EDEALAQAGR
WAAETGVAVL VKTGHLEDRE VTNTWVEPDG SQHRASSARV ETTSTHGTGC SLASALATRL
GAGHRPAAAL AWATQWLHEA IVHGAALQVG TGHGPVDHAH QGRRLAAAGS AAPWLRVGEV
PARLEAPEDL IDACSGDAGT ETGIAPVLPV VAPAGPWTAA LWAAGSSLAA QVADSGFVRA
LVDGSLPGPA FDVYLAQDAL YLARYSRALA ALAEASTTAS GRTFWAESSR SCLTVEAELH
RSWLSAEPAE DDTALSPVTS AYTDFLLRHA LGSPTPVVAA AVLPCFWLYA QVGGELAEIA
PGHPYAAWLE TYRDPGFVEG VQGALGEVER ELAAASPVRR AAAARAFLLA CRHELEFFEQ
ARRLAPHDAP AEAALSGAVR
//
