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PK21B_CORGL
ID   PK21B_CORGL             Reviewed;         306 AA.
AC   Q8NM65;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Polyphosphate kinase PPK2B {ECO:0000305};
DE            EC=2.7.4.1 {ECO:0000269|PubMed:17545325};
GN   Name=ppk2B {ECO:0000303|PubMed:17545325};
GN   OrderedLocusNames=Cgl2714 {ECO:0000312|EMBL:BAC00108.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=17545325; DOI=10.1128/aem.00600-07;
RA   Lindner S.N., Vidaurre D., Willbold S., Schoberth S.M., Wendisch V.F.;
RT   "NCgl2620 encodes a class II polyphosphate kinase in Corynebacterium
RT   glutamicum.";
RL   Appl. Environ. Microbiol. 73:5026-5033(2007).
CC   -!- FUNCTION: Catalyzes the synthesis of polyP from ATP or GTP. Can also
CC       use inorganic polyphosphate (polyP) as a donor to convert ADP to ATP,
CC       but the activity is 10-fold higher in vitro for polyP synthesis than
CC       for ATP formation. {ECO:0000269|PubMed:17545325}.
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; EC=2.7.4.1;
CC         Evidence={ECO:0000269|PubMed:17545325};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19574;
CC         Evidence={ECO:0000269|PubMed:17545325};
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:17545325};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55413;
CC         Evidence={ECO:0000269|PubMed:17545325};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:17545325};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.17 mM for ATP {ECO:0000269|PubMed:17545325};
CC         KM=0.14 mM for GTP {ECO:0000269|PubMed:17545325};
CC         KM=15 mM for polyP {ECO:0000269|PubMed:17545325};
CC         KM=0.04 mM for ADP {ECO:0000269|PubMed:17545325};
CC         Vmax=31 umol/min/mg enzyme with ATP as substrate for polyP formation
CC         {ECO:0000269|PubMed:17545325};
CC         Vmax=14 umol/min/mg enzyme with GTP as substrate for polyP formation
CC         {ECO:0000269|PubMed:17545325};
CC         Vmax=4 umol/min/mg enzyme with ADP as substrate for ATP formation
CC         {ECO:0000269|PubMed:17545325};
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:17545325};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17545325}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant accumulates very little cellular
CC       polyP. {ECO:0000269|PubMed:17545325}.
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC       I subfamily. {ECO:0000305}.
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DR   EMBL; BA000036; BAC00108.1; -; Genomic_DNA.
DR   RefSeq; NP_601909.1; NC_003450.3.
DR   AlphaFoldDB; Q8NM65; -.
DR   SMR; Q8NM65; -.
DR   STRING; 196627.cg3007; -.
DR   KEGG; cgl:Cgl2714; -.
DR   PATRIC; fig|196627.13.peg.2645; -.
DR   eggNOG; COG2326; Bacteria.
DR   HOGENOM; CLU_048699_2_2_11; -.
DR   OMA; TKLWFSV; -.
DR   BRENDA; 2.7.4.1; 960.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
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   Kinase; Manganese; Reference proteome; Transferase.
FT   CHAIN           1..306
FT                   /note="Polyphosphate kinase PPK2B"
FT                   /id="PRO_0000442584"
SQ   SEQUENCE   306 AA;  36044 MW;  667C0E8860432986 CRC64;
     MVGKLPIMAE TNENDLPVID LAQIEGYVVD DSDEDDPVLL RPDGTPIETW REDFPYEERV
     TREDYEKVKR SLQIELLKWQ NWTKETGQRH IILFEGRDAA GKGGTIKRFN EHLNPRGART
     VALEKPSPRE STSWYFQRYI QHFPAAGEIV FFDRSWYNRS GVERVMGFCT ESQHAEFLRE
     VPMLENMILG SGISLTKFWF SVTRKEQRTR FAIRQVDPVR QWKLSPMDLA SLDRWDDYTR
     AKEEQFRYTD TDESPWITIK SNDKKRARIN AMRYVLSKFD YTDKDYELVG EPDPKVVLRG
     RDQIGD
 
 
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