位置:首页 > 蛋白库 > PPK1_MYCGI
PPK1_MYCGI
ID   PPK1_MYCGI              Reviewed;         729 AA.
AC   A4TE29;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347};
DE            EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE   AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00347};
DE   AltName: Full=Polyphosphoric acid kinase {ECO:0000255|HAMAP-Rule:MF_00347};
GN   Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347}; OrderedLocusNames=Mflv_4223;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       of ATP to form a long-chain polyphosphate (polyP). {ECO:0000255|HAMAP-
CC       Rule:MF_00347}.
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:0000255|HAMAP-Rule:MF_00347};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC   -!- PTM: An intermediate of this reaction is the autophosphorylated ppk in
CC       which a phosphate is covalently linked to a histidine residue through a
CC       N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347}.
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00347}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000656; ABP46692.1; -; Genomic_DNA.
DR   RefSeq; WP_011895067.1; NC_009338.1.
DR   AlphaFoldDB; A4TE29; -.
DR   SMR; A4TE29; -.
DR   STRING; 350054.Mflv_4223; -.
DR   EnsemblBacteria; ABP46692; ABP46692; Mflv_4223.
DR   KEGG; mgi:Mflv_4223; -.
DR   eggNOG; COG0855; Bacteria.
DR   HOGENOM; CLU_009678_5_0_11; -.
DR   OMA; NIKWARK; -.
DR   OrthoDB; 76567at2; -.
DR   GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1840.10; -; 1.
DR   HAMAP; MF_00347; Polyphosphate_kinase; 1.
DR   InterPro; IPR003414; PP_kinase.
DR   InterPro; IPR041108; PP_kinase_C_1.
DR   InterPro; IPR024953; PP_kinase_middle.
DR   InterPro; IPR036830; PP_kinase_middle_dom_sf.
DR   InterPro; IPR025200; PPK_C_dom2.
DR   InterPro; IPR025198; PPK_N_dom.
DR   InterPro; IPR036832; PPK_N_dom_sf.
DR   PANTHER; PTHR30218; PTHR30218; 1.
DR   Pfam; PF02503; PP_kinase; 1.
DR   Pfam; PF13090; PP_kinase_C; 1.
DR   Pfam; PF17941; PP_kinase_C_1; 1.
DR   Pfam; PF13089; PP_kinase_N; 1.
DR   PIRSF; PIRSF015589; PP_kinase; 1.
DR   SUPFAM; SSF140356; SSF140356; 1.
DR   TIGRFAMs; TIGR03705; poly_P_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN           1..729
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_1000079365"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        482
FT                   /note="Phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         422
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ   SEQUENCE   729 AA;  81242 MW;  107DFC5C95A19090 CRC64;
     MTEAQTRTEP SESSESSEAV APAITSAADS APEAPPATTA PAIENPLPED RYLNRELSWL
     DFNARVLALA ADPSLPLLER AKFLAIFASN LDEFYMVRVA GLKRRDEMGL SVRSADGLSP
     REQLRRISER TQQIASRHAH VFLDSVRPAL ADEGIVIVTW AQLDDAERAK LSTYFHEQVF
     PVLTPLAVDP AHPFPFVSGL SLNLAITVKH PDDGGQHFAR IKVPDNVDRF VELPARGDSP
     GVVRFLPMEE LIAAFLTVLF PGLEIVEHHA FRITRNADFE VEEDRDEDLL QALERELARR
     RFGSPVRLEV SDDMTESMLE LLLRELDVAP GDVVEVPGLL DLSSLWQIYS VDRPGLKDPP
     FVPATPSAFG ERETPKSIFS ALRDGDVLVH HPYDSFSTTV QRFIEQAAAD PNVLAIKQTL
     YRTSGDSPIV NALIDAAEAG KQVVALVEIK ARFDEQANIK WARALEQAGV HVVYGLIGLK
     THCKTCLVVR REGSTIRRYC HIGTGNYNPK TARLYEDIGL LTAAPDIGAD LTDLFNSLTG
     YSRKESYRNL LVAPYGVRRG IIERIDREIA ATRDGAEGRI RLKANALVDE QVIDALYRAS
     QAGVQVEVVV RGICALRPGE PGFSDNITVR SILGRFLEHS RIIHFRAIDE YWIGSADMMH
     RNLDRRVEVM AQVKDPRLTT QLNDIFDSAA DPRTRCWELG SDGHWTALPQ EGHSVRDHQI
     SLMERRRHP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024