ID C7GET1_9FIRM Unreviewed; 730 AA.
AC C7GET1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 Name=ppdK {ECO:0000313|EMBL:EEU99662.1};
GN ORFNames=ROSINTL182_08433 {ECO:0000313|EMBL:EEU99662.1};
OS Roseburia intestinalis L1-82.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=536231 {ECO:0000313|EMBL:EEU99662.1, ECO:0000313|Proteomes:UP000004828};
RN [1] {ECO:0000313|EMBL:EEU99662.1, ECO:0000313|Proteomes:UP000004828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L1-82 {ECO:0000313|EMBL:EEU99662.1,
RC ECO:0000313|Proteomes:UP000004828};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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:EEU99662.1}.
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; ABYJ02000187; EEU99662.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GET1; -.
DR HOGENOM; CLU_015345_0_0_9; -.
DR Proteomes; UP000004828; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.20.80.30; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 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; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01828; pyru_phos_dikin; 1.
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 Pfam; PF01326; PPDK_N; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:EEU99662.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:EEU99662.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEU99662.1}.
FT DOMAIN 55..142
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 160..207
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 275..356
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 373..723
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 730 AA; 80357 MW; 6F897AB15FB18776 CRC64;
MVKKYFEQLI DKMKEERGVK FDIDLTAADL KELAEQFKTE YKNQLGTDFP SDPVEQLKLA
IEAVFRSWDN PRANVYRRDN DIPYSWGTAV NVMPMVFGNL NNESGTGVAF TRDPATGENK
LMGEFLINAQ GEDVVAGVRT PMPIAQMEKE FPEAYADFLK VCETLENHYH DMQDMEFTVE
NKKLYMLQCR NGKRTAPAAL KIACDLVDEG HKTPEEAVAM IDPRNLDTLL HPQFDAAALK
AATPIGKGLG ASPGAACGKI VFTAEDAEEW NARGEKVVLV RLETSPEDIT GMKASQGILT
VRGGMTSHAA VVARGMGTCC VSGCGDIAMD EENKKFTLAG KEFHEGDYIS IDGTTGNIYD
GAIKTVDATI AGEFGRVMAW ADQFRTLKVR TNADTPADAK KARELGAEGI GLCRTEHMFF
EEDRIAAFRE MICSDTVEER EAALEKILPY QQGDFEALYE ALEGNPVTIR FLDPPLHEFV
PTEEADIEKL AKAQGKSVET IKNIIASLHE FNPMMGHRGC RLAVTYPEIA KMQTKAVIRA
AINVQKKHAD WTVKPEIMIP LVCEVKELKY VKDVVVETAD AEIAAAGIKL EYEVGTMIEI
PRAALTADEI AKEADFFCFG TNDLTQMTYG FSRDDAGKFL NAYYDKKIFE NDPFAKLDQT
GVGKLMETAI KLGKPVNPKL HVGICGEHGG DPSSVEFCHK IGLDYVSCSP FRVPIARLAA
AQAAIANAGK
//
