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Database: UniProt
Entry: W4V7F8_9FIRM
LinkDB: W4V7F8_9FIRM
Original site: W4V7F8_9FIRM 
ID   W4V7F8_9FIRM            Unreviewed;       220 AA.
AC   W4V7F8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE            EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE   AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
GN   ORFNames=JCM21531_2221 {ECO:0000313|EMBL:GAE88748.1};
OS   Acetivibrio straminisolvens JCM 21531.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE88748.1, ECO:0000313|Proteomes:UP000019109};
RN   [1] {ECO:0000313|EMBL:GAE88748.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE88748.1};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT   Isolated from a Cellulose-Degrading Bacterial Community.";
RL   Genome Announc. 2:e00110-14(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE88748.1}.
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DR   EMBL; BAVR01000024; GAE88748.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4V7F8; -.
DR   STRING; 1294263.JCM21531_2221; -.
DR   Proteomes; UP000019109; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:GAE88748.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:GAE88748.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..110
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          125..217
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   220 AA;  24174 MW;  39E78FED17DFF7B8 CRC64;
     MPASPGAATG KVYFSAEDAV EAAKSGEKNI ILVRLETSPE DIEGMHVSKG ILTGRGGMTS
     HAAVVARGMG TCCVAGCSEI RINEEEKYFI DKNGKKYVEG DWISLDGSTG NVYGQKLPTV
     EPEMTGDFAT LMQWADEIRT LKIRTNADTP ADAIQARKFG AEGIGLCRTE HMFFDSDRIP
     AMREMIVSRN EEQRRKALDK LLPMQRGDFE ELFTAMEAIL
//
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