PK21A_RHIME
ID PK21A_RHIME Reviewed; 300 AA.
AC Q92SA6;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ADP-polyphosphate phosphotransferase 1 {ECO:0000305};
DE EC=2.7.4.- {ECO:0000269|PubMed:19001261};
DE AltName: Full=Polyphosphate kinase PPK2 1 {ECO:0000305};
GN ORFNames=SMc02148 {ECO:0000312|EMBL:CAC41944.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3] {ECO:0007744|PDB:3CZQ}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF
RP GLU-90; ASP-93; LYS-97; ASP-148; ARG-149; TRP-194; GLN-202; ARG-205;
RP ARG-209; ASP-223; TYR-233 AND ARG-263.
RX PubMed=19001261; DOI=10.1073/pnas.0807563105;
RA Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J.,
RA Edwards A.M., Savchenko A., Joachimiak A., Yakunin A.F.;
RT "Polyphosphate-dependent synthesis of ATP and ADP by the family-2
RT polyphosphate kinases in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17730-17735(2008).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC ADP to ATP. Can also convert GDP to GTP, with lower efficiency. Cannot
CC dephosphorylate ATP in the presence of polyP.
CC {ECO:0000269|PubMed:19001261}.
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:19001261};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19575;
CC Evidence={ECO:0000269|PubMed:19001261};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + GTP = [phosphate](n+1) + GDP;
CC Xref=Rhea:RHEA:55412, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:19001261};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55414;
CC Evidence={ECO:0000269|PubMed:19001261};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19001261};
CC Note=Has low activity with Co(2+) or Ni(2+).
CC {ECO:0000269|PubMed:19001261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for polyP {ECO:0000269|PubMed:19001261};
CC KM=32 uM for ADP {ECO:0000269|PubMed:19001261};
CC KM=520 uM for GDP {ECO:0000269|PubMed:19001261};
CC Note=kcat is 8.6 sec(-1) with polyP as substrate. kcat is 7.6 sec(-1)
CC with ADP as substrate. kcat is 0.8 sec(-1) with GDP as substrate.
CC {ECO:0000269|PubMed:19001261};
CC pH dependence:
CC Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:19001261};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19001261}.
CC -!- INTERACTION:
CC Q92SA6; Q92SA6: SMc02148; NbExp=2; IntAct=EBI-15739743, EBI-15739743;
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC I subfamily. {ECO:0000305}.
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DR EMBL; AL591688; CAC41944.1; -; Genomic_DNA.
DR RefSeq; NP_384613.1; NC_003047.1.
DR RefSeq; WP_010968631.1; NC_003047.1.
DR PDB; 3CZQ; X-ray; 2.23 A; A/B/C/D=1-300.
DR PDB; 6DZG; X-ray; 1.87 A; A/B/C/D=1-300.
DR PDBsum; 3CZQ; -.
DR PDBsum; 6DZG; -.
DR AlphaFoldDB; Q92SA6; -.
DR SMR; Q92SA6; -.
DR DIP; DIP-48619N; -.
DR STRING; 266834.SMc02148; -.
DR EnsemblBacteria; CAC41944; CAC41944; SMc02148.
DR GeneID; 61601981; -.
DR KEGG; sme:SMc02148; -.
DR PATRIC; fig|266834.11.peg.1880; -.
DR eggNOG; COG2326; Bacteria.
DR HOGENOM; CLU_048699_2_0_5; -.
DR OMA; TKLWFSV; -.
DR BRENDA; 2.7.4.1; 5347.
DR EvolutionaryTrace; Q92SA6; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022488; PPK2-related.
DR InterPro; IPR022486; PPK2_PA0141.
DR Pfam; PF03976; PPK2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03707; PPK2_P_aer; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Kinase; Magnesium; Reference proteome;
KW Transferase.
FT CHAIN 1..300
FT /note="ADP-polyphosphate phosphotransferase 1"
FT /id="PRO_0000442589"
FT MUTAGEN 90
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 93
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 97
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 148
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 149
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 194
FT /note="W->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 202
FT /note="Q->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 205
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 209
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 223
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 233
FT /note="Y->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT MUTAGEN 263
FT /note="R->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:19001261"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3CZQ"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6DZG"
FT TURN 41..48
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 57..81
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6DZG"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 166..186
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:6DZG"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:6DZG"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6DZG"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6DZG"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6DZG"
SQ SEQUENCE 300 AA; 34847 MW; EA6993AD74C98EA6 CRC64;
MALDEAPAEA RPGSRAVELE IDGRSRIFDI DDPDLPKWID EEAFRSDDYP YKKKLDREEY
EETLTKLQIE LVKVQFWMQA TGKRVMAVFE GRDAAGKGGA IHATTANMNP RSARVVALTK
PTETERGQWY FQRYVATFPT AGEFVLFDRS WYNRAGVEPV MGFCTPDQYE QFLKEAPRFE
EMIANEGIHL FKFWINIGRE MQLKRFHDRR HDPLKIWKLS PMDIAALSKW DDYTGKRDRM
LKETHTEHGP WAVIRGNDKR RSRINVIRHM LTKLDYDGKD EAAIGEVDEK ILGSGPGFLR
