PK23_MEIRD
ID PK23_MEIRD Reviewed; 267 AA.
AC M9XB82;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=AMP/ADP-polyphosphate phosphotransferase {ECO:0000305};
DE EC=2.7.4.- {ECO:0000269|PubMed:24532069};
GN ORFNames=K649_10090;
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Meiothermus.
OX NCBI_TaxID=504728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21;
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-126.
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21;
RX PubMed=24532069; DOI=10.1128/aem.03971-13;
RA Motomura K., Hirota R., Okada M., Ikeda T., Ishida T., Kuroda A.;
RT "A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both
RT nucleoside monophosphate phosphorylation and nucleoside diphosphate
RT phosphorylation.";
RL Appl. Environ. Microbiol. 80:2602-2608(2014).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC both AMP to ADP and ADP to ATP. Can also use GMP, CMP, UMP, GDP, CDP
CC and UDP. {ECO:0000269|PubMed:24532069}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ADP = [phosphate](n+1) + AMP;
CC Xref=Rhea:RHEA:57820, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24532069};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57822;
CC Evidence={ECO:0000269|PubMed:24532069};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24532069};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19575;
CC Evidence={ECO:0000269|PubMed:24532069};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24532069};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 60-70 degrees Celsius.
CC {ECO:0000269|PubMed:24532069};
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC III subfamily. {ECO:0000305}.
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DR EMBL; CP005385; AGK05310.1; -; Genomic_DNA.
DR RefSeq; WP_015586734.1; NC_021081.1.
DR PDB; 5MAQ; X-ray; 2.46 A; A/B/C/D=1-267.
DR PDB; 5O6K; X-ray; 2.90 A; A/B/C/D=1-267.
DR PDB; 5O6M; X-ray; 2.30 A; A/B/C/D=1-267.
DR PDBsum; 5MAQ; -.
DR PDBsum; 5O6K; -.
DR PDBsum; 5O6M; -.
DR AlphaFoldDB; M9XB82; -.
DR SMR; M9XB82; -.
DR STRING; 504728.K649_10090; -.
DR EnsemblBacteria; AGK05310; AGK05310; K649_10090.
DR KEGG; mre:K649_10090; -.
DR PATRIC; fig|504728.9.peg.2081; -.
DR eggNOG; COG2326; Bacteria.
DR OrthoDB; 953793at2; -.
DR BRENDA; 2.7.4.1; 6338.
DR BRENDA; 2.7.4.34; 6338.
DR Proteomes; UP000013026; Chromosome.
DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006797; P:polyphosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016898; Polyphosphate_phosphotransfera.
DR InterPro; IPR022300; PPK2-rel_1.
DR InterPro; IPR022488; PPK2-related.
DR Pfam; PF03976; PPK2; 1.
DR PIRSF; PIRSF028756; PPK2_prd; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03709; PPK2_rel_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Kinase; Manganese; Transferase.
FT CHAIN 1..267
FT /note="AMP/ADP-polyphosphate phosphotransferase"
FT /id="PRO_0000442599"
FT MUTAGEN 126
FT /note="E->G: 6-fold decrease in synthesis of ATP from AMP."
FT /evidence="ECO:0000269|PubMed:24532069"
FT MUTAGEN 126
FT /note="E->N: 20-fold decrease in synthesis of ATP from AMP.
FT 7-fold decrease in synthesis of ATP from ADP."
FT /evidence="ECO:0000269|PubMed:24532069"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5O6K"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 29..53
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:5O6M"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:5O6M"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5O6M"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:5O6M"
FT HELIX 232..249
FT /evidence="ECO:0007829|PDB:5O6M"
SQ SEQUENCE 267 AA; 31559 MW; C3C95B21F68C3293 CRC64;
MKKYRVQPDG RFELKRFDPD DTSAFEGGKQ AALEALAVLN RRLEKLQELL YAEGQHKVLV
VLQAMDAGGK DGTIRVVFDG VNPSGVRVAS FGVPTEQELA RDYLWRVHQQ VPRKGELVIF
NRSHYEDVLV VRVKNLVPQQ VWQKRYRHIR EFERMLADEG TTILKFFLHI SKDEQRQRLQ
ERLDNPEKRW KFRMGDLEDR RLWDRYQEAY EAAIRETSTE YAPWYVIPAN KNWYRNWLVS
HILVETLEGL AMQYPQPETA SEKIVIE
