ID D5ECW8_AMICL Unreviewed; 281 AA.
AC D5ECW8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ADE56400.1};
GN OrderedLocusNames=Amico_0255 {ECO:0000313|EMBL:ADE56400.1};
OS Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminobacterium.
OX NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56400.1, ECO:0000313|Proteomes:UP000002366};
RN [1] {ECO:0000313|EMBL:ADE56400.1, ECO:0000313|Proteomes:UP000002366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX PubMed=21304712;
RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT 1).";
RL Stand. Genomic Sci. 2:280-289(2010).
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}.
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DR EMBL; CP001997; ADE56400.1; -; Genomic_DNA.
DR RefSeq; WP_013047666.1; NC_014011.1.
DR AlphaFoldDB; D5ECW8; -.
DR STRING; 572547.Amico_0255; -.
DR KEGG; aco:Amico_0255; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_1_0; -.
DR OMA; DNRHTHG; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000002366; Chromosome.
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:ADE56400.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002366};
KW Transferase {ECO:0000313|EMBL:ADE56400.1}.
FT DOMAIN 15..262
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 281 AA; 29911 MW; A57E42B8FB1586E0 CRC64;
MALYRGNALT IAGSDSGGGA GIQADLKTFA ALHIFGMSVI TAVTAQNSLT VKDIHDIPPK
SITAQLDAVL SDFRVDAAKT GMLSRPETIH VVCEALKNYQ LSNLVVDPVM ISQSGVSLIS
ESAVQALKEQ LLPLALLVTP NMPEAEKLSG VEVQSLEDMK NAARLISGLG PKAVLVKGGH
MDVEKSKEKV VDVLYCEGKI TIFEDPRVDT ENTHGTGCTL SAAIAAELSA GRDLEEAVSY
GRQYLRMGLL HSFKPGHGYG PLGHAVTPEW VKEYESGDNE I
//