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Database: UniProt
Entry: K7A271_9ALTE
LinkDB: K7A271_9ALTE
Original site: K7A271_9ALTE 
ID   K7A271_9ALTE            Unreviewed;       522 AA.
AC   K7A271;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGH47384.1};
GN   ORFNames=C427_5287 {ECO:0000313|EMBL:AGH47384.1};
OS   Paraglaciecola psychrophila 170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH47384.1, ECO:0000313|Proteomes:UP000011864};
RN   [1] {ECO:0000313|EMBL:AGH47384.1, ECO:0000313|Proteomes:UP000011864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:AGH47384.1,
RC   ECO:0000313|Proteomes:UP000011864};
RX   PubMed=23640379;
RA   Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT   "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL   Genome Announc. 1:E00199-13(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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; CP003837; AGH47384.1; -; Genomic_DNA.
DR   RefSeq; WP_007635877.1; NZ_BAES01000019.1.
DR   AlphaFoldDB; K7A271; -.
DR   STRING; 1129794.C427_5287; -.
DR   KEGG; gps:C427_5287; -.
DR   PATRIC; fig|1129794.4.peg.5270; -.
DR   eggNOG; COG0351; Bacteria.
DR   eggNOG; COG0352; Bacteria.
DR   HOGENOM; CLU_018272_7_1_6; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000011864; Chromosome.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
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; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011864};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT   DOMAIN          27..283
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
FT   DOMAIN          330..501
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
SQ   SEQUENCE   522 AA;  56741 MW;  54ECE31C7468A0DF CRC64;
     MDNYSNDNRL FVSGCDRPIV WSIAASDSGG GAGIQADTLT IQDLGGHACN IITAVTVQNS
     YHVEGVSAVS PDMLTRQLNC LLFDMPPKVI KIGVLADAEQ VLLISNWLAD NLADYEQTHD
     TRIPIILDPV LFTTSGKQQT NVDAYLRLAK QVTLLTPNYN ELMVLAGTFE GKGQTEQSAL
     DHLSQLVETN ILVTGGDSQN LQVVDWLAAH KIAHTSEQHQ HQRIGFGGSR VNTRHNHGTG
     CTLSSAIATT MALGHPLLDA IVIAKAYVHQ GLSGSYGLGK GPGVLARHGW PNDLVHFPEI
     ILPQYPQLAD VSQLDFANVS LPLKVYSVTQ SLSVLEQVLK AGAHTAQLRI KLPCDNKQLE
     QDIQLAVALG RKYQAQVFIN DHWQLAIKHG AFGIHLGQED MLQANLSQIS DASLALGLSS
     HGYFEMLLAQ QFSPSYLAIG HIFATPTKHM PSQPQGLLKL SRYCQLLKDK LPLVAIGGID
     EHNLAQVKVT QVHDVAIVRG IELAPDPAKS WQTLQLAWQA LT
//
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