ID D7BK03_ARCHD Unreviewed; 537 AA.
AC D7BK03;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ADH92983.1};
GN OrderedLocusNames=Arch_1278 {ECO:0000313|EMBL:ADH92983.1};
OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / CCUG 17215 /
OS LMG 16163 / NBRC 15585 / NCTC 8452 / 11018).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Arcanobacterium.
OX NCBI_TaxID=644284 {ECO:0000313|EMBL:ADH92983.1, ECO:0000313|Proteomes:UP000000376};
RN [1] {ECO:0000313|EMBL:ADH92983.1, ECO:0000313|Proteomes:UP000000376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9345 / DSM 20595 / CCUG 17215 / LMG 16163 / NBRC 15585 /
RC NCTC 8452 / 11018 {ECO:0000313|Proteomes:UP000000376};
RX PubMed=21304742; DOI=10.4056/sigs.1123072;
RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Rohde M., Sikorski J., Pukall R., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Arcanobacterium haemolyticum type strain
RT (11018).";
RL Stand. Genomic Sci. 3:126-135(2010).
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; CP002045; ADH92983.1; -; Genomic_DNA.
DR RefSeq; WP_013170475.1; NC_014218.1.
DR AlphaFoldDB; D7BK03; -.
DR STRING; 644284.Arch_1278; -.
DR KEGG; ahe:Arch_1278; -.
DR eggNOG; COG0351; Bacteria.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_020520_2_0_11; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000000376; 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:ADH92983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000376};
KW Transferase {ECO:0000313|EMBL:ADH92983.1}.
FT DOMAIN 13..262
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 344..535
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 537 AA; 58322 MW; 5F52D30245BFC362 CRC64;
MSIPRILTIA GTDPSGGAGA QADIKSITAT GGFAYSVVTA IVAQNTQGVR SIFSPPPSVI
RDQLEALNDD VVIDAVKIGM LGNTGYIQIV DEWLDGHKPP IVVVDPVMVA TSGDRLLDTE
AEDALKNMLH HATVVTPNIP ELEILAQLAP GTIQNHSDAI AAAQKLARDI NATVLVKGGH
LTERIVTNAL VDAEGVITEA HTERVDTDAT HGTGCSLSSA LATRLAAEGN ATRALGWVTD
WLHEAISYGE KLQVGTGHGP VDHSHKLRRM EASIPAQPWL PAPTPLATPE SARATDVAQT
RIFRQNGKPT EWDVRTPRIA PAGPWTTLLW NATQDVVEDT WELPFIQQLA AGTLPYWQFT
AYQRQDALYL DTYVRALAHL AARATEPADV AAWAQSSAEC VIVEQELHRN WLTKHSDAIP
ESSYAMSPVT TGYTDHLLAR TSTDPYVVGV AAVLPCFWIY AHIGELLAEA NTPTHPYHEW
LSMYSDQGFI DATAHRIRLM EKALAGATPE ERAAALQAYS VAARWECEFF DQARRMR
//
