PK22_ACIJO
ID PK22_ACIJO Reviewed; 475 AA.
AC Q83XD3;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Polyphosphate:AMP phosphotransferase {ECO:0000303|PubMed:1655714};
DE Short=PAP {ECO:0000303|PubMed:15262957};
DE EC=2.7.4.33 {ECO:0000269|PubMed:15262957, ECO:0000269|PubMed:15716459, ECO:0000269|PubMed:1655714};
DE AltName: Full=Polyphosphate kinase PPK2 {ECO:0000305};
GN Name=pap {ECO:0000303|PubMed:15716459};
OS Acinetobacter johnsonii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=40214;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=210A;
RX PubMed=15716459; DOI=10.1128/jb.187.5.1859-1865.2005;
RA Shiba T., Itoh H., Kameda A., Kobayashi K., Kawazoe Y., Noguchi T.;
RT "Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent
RT nucleoside monophosphate kinase in Acinetobacter johnsonii 210A.";
RL J. Bacteriol. 187:1859-1865(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=210A;
RX PubMed=1655714; DOI=10.1128/jb.173.20.6484-6488.1991;
RA Bonting C.F., Kortstee G.J., Zehnder A.J.;
RT "Properties of polyphosphate:AMP phosphotransferase of Acinetobacter strain
RT 210A.";
RL J. Bacteriol. 173:6484-6488(1991).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=210A;
RX PubMed=15262957; DOI=10.1128/jb.186.15.5178-5181.2004;
RA Itoh H., Shiba T.;
RT "Polyphosphate synthetic activity of polyphosphate:AMP phosphotransferase
RT in Acinetobacter johnsonii 210A.";
RL J. Bacteriol. 186:5178-5181(2004).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC AMP to ADP. Can also use GMP, UMP, CMP, TMP or deoxyribonucleoside
CC monophosphates, with lower efficiency. Cannot use low-molecular weight
CC polyP as donors. Can also catalyze the synthesis of polyP from ADP or
CC GDP, with lower efficiency. {ECO:0000269|PubMed:15262957,
CC ECO:0000269|PubMed:15716459, ECO:0000269|PubMed:1655714}.
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 EC=2.7.4.33; Evidence={ECO:0000269|PubMed:15262957,
CC ECO:0000269|PubMed:15716459, ECO:0000269|PubMed:1655714};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15262957, ECO:0000269|PubMed:15716459};
CC Note=Lower concentrations of MgCl(2) are required to obtain optimum
CC polyP synthetic activity, whereas higher concentrations of MgCl(2) are
CC necessary for optimum PAP activity. {ECO:0000269|PubMed:15262957,
CC ECO:0000269|PubMed:15716459};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for AMP {ECO:0000269|PubMed:1655714};
CC KM=4.4 mM for GMP {ECO:0000269|PubMed:15716459};
CC KM=0.8 uM for polyP {ECO:0000269|PubMed:1655714};
CC KM=8.3 mM for ADP {ECO:0000269|PubMed:15262957};
CC Vmax=180 umol/min/mg enzyme with AMP as substrate for ADP formation
CC {ECO:0000269|PubMed:15262957, ECO:0000269|PubMed:15716459};
CC Vmax=37 umol/min/mg enzyme with GMP as substrate for GDP formation
CC {ECO:0000269|PubMed:15716459};
CC Vmax=55 umol/min/mg enzyme with ADP as substrate for polyP formation
CC {ECO:0000269|PubMed:15262957};
CC pH dependence:
CC Optimum pH is 6.5-8.5 (PubMed:1655714). Optimum pH is 8.0-9.0
CC (PubMed:15716459). {ECO:0000269|PubMed:15716459,
CC ECO:0000269|PubMed:1655714};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:15716459};
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000269|PubMed:15716459}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC II subfamily. {ECO:0000305}.
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DR EMBL; AB092983; BAC76403.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83XD3; -.
DR SMR; Q83XD3; -.
DR BRENDA; 2.7.4.1; 103.
DR BRENDA; 2.7.4.33; 103.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022488; PPK2-related.
DR Pfam; PF03976; PPK2; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Kinase; Magnesium; Repeat; Transferase.
FT CHAIN 1..475
FT /note="Polyphosphate:AMP phosphotransferase"
FT /id="PRO_0000442596"
FT REGION 18..222
FT /note="PPK2 1"
FT /evidence="ECO:0000305"
FT REGION 256..472
FT /note="PPK2 2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 55838 MW; 972FE2A76CCCEE01 CRC64;
MDTETIASAV LNEEQLSLDL IEAQYALMNT RDQSNAKSLV ILVSGIELAG KGEAVKQLRE
WVDPRFLYVK ADPPHLFNLK QPFWQPYTRF VPAEGQIMVW FGNWYGDLLA TAMHASKPLD
DTLFDEYVSN MRAFEQDLKN NNVDVLKVWF DLSWKSLQKR LDDMDPSEVH WHKLHGLDWR
NKKQYDTLQK LRTRFTDDWQ IIDGEDEDLR NHNFAQAILT ALRHCPEHEK KAALKWQQAP
IPDILTQFEV PQAEDANYKS ELKKLTKQVA DAMRCDDRKV VIAFEGMDAA GKGGAIKRIV
KKLDPREYEI HTIAAPEKYE LRRPYLWRFW SKLQSDDITI FDRTWYGRVL VERVEGFATE
VEWQRAYAEI NRFEKNLSSS QTVLIKFWLA IDKDEQAARF KARESTPHKR FKITEEDWRN
RDKWDDYLKA AADMFAHTDT SYAPWYIIST NDKQQARIEV LRAILKQLKA DRDTD
