ID U5T3A8_9GAMM Unreviewed; 276 AA.
AC U5T3A8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pyridoxamine kinase/Phosphomethylpyrimidine kinase domain-containing protein {ECO:0000259|Pfam:PF08543};
GN ORFNames=SPICUR_04760 {ECO:0000313|EMBL:AGY91930.1};
OS Spiribacter curvatus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=1335757 {ECO:0000313|EMBL:AGY91930.1, ECO:0000313|Proteomes:UP000017640};
RN [1] {ECO:0000313|EMBL:AGY91930.1, ECO:0000313|Proteomes:UP000017640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAH-SP71 {ECO:0000313|EMBL:AGY91930.1,
RC ECO:0000313|Proteomes:UP000017640};
RX PubMed=24225341; DOI=10.1186/1471-2164-14-787;
RA Lopez-Perez M., Ghai R., Leon M.J., Rodriguez-Olmos A., Copa-Patino J.L.,
RA Soliveri J., Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "Genomes of "Spiribacter", a streamlined, successful halophilic
RT bacterium.";
RL BMC Genomics 14:787-787(2013).
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; CP005990; AGY91930.1; -; Genomic_DNA.
DR RefSeq; WP_023366581.1; NC_022664.1.
DR AlphaFoldDB; U5T3A8; -.
DR STRING; 1335757.SPICUR_04760; -.
DR KEGG; spiu:SPICUR_04760; -.
DR PATRIC; fig|1335757.3.peg.927; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_3_6; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000017640; Chromosome.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 Reference proteome {ECO:0000313|Proteomes:UP000017640}.
FT DOMAIN 13..258
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 251..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 28824 MW; 59CD7CAAA5CF94B5 CRC64;
MSPARILIIA GSDSGGGAGI QADIKTVTAL GGYAMTAVTA LTAQNTEGVQ GVVGIEPGFI
REQIRSVVDD LGVDCVKTGM LHDRAVIDAV ADELERFAGH VPWVIDPVMV AQSGARLVAD
DGMAYLRDRL IPNARLITPN IPEAQALLGR PIESPAAMDE AARALLALGC EAVLLKGGHL
DGDTLIDVLA TAGGNQRFEH PRIATTSDHG TGCTLASAIA EGLGRELPLD AAVHRGRDYL
HEALVTASSL GHGHGPVNHT HTVSPYRLTA TDQYRT
//
