ID A0A1C2HBT5_9RHOB Unreviewed; 845 AA.
AC A0A1C2HBT5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BFP70_16495 {ECO:0000313|EMBL:OCX61206.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX61206.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX61206.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX61206.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
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:OCX61206.1}.
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DR EMBL; MDHA01000069; OCX61206.1; -; Genomic_DNA.
DR RefSeq; WP_066012940.1; NZ_MDHA01000069.1.
DR AlphaFoldDB; A0A1C2HBT5; -.
DR STRING; 1889770.BFP70_16495; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000094269; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 3.30.1490.20; ATP-grasp fold, A 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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
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 PIRSF; PIRSF000853; PPDK; 1.
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; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:OCX61206.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3}; Pyruvate {ECO:0000313|EMBL:OCX61206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094269};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 388..471
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 489..836
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 422
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 798
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 529
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 585
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 712
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 712
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 734
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 735
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 736
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 736
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 845 AA; 92064 MW; 8ABFBFA744E62D6C CRC64;
MQKHYEFDEF VELRPTAKVD KSRHGWRAKC LQRLIRLDLP VPATVALPTE TVRRIAAGQM
PDVAAIIECF GDEMLISVRS SPENPEWGGP GTVLNVGLNN DMHARLVETH GAEAADALYL
AFVQNYAVHV ARLDPDMFCA PAGPGAVQAA LAMYQEEMDS EFPQNPVQQL IEVLRSMARA
WEGTTARLLR QAKGAPAEAT LGLVLQQMAL GIGPGLSGSG TIQFVDSVTG KPLINGRFRR
QSQGRASADA ELYLTRDPRG PSLEDLAPEV FEQLRGYGAI CRQRLREEMQ VEFTLEGGRV
SVIDAVRVQR SARAGVRIAV ALAEDGVIPR EDALLRVEPR ALTELLHFQV DPRAPRDVLA
RGIAASPGAA TGKIVFSAAA AQASAARDEP CILVRRETSP EDVRGMHAAH AVLTERGGMT
SHAAVIARGL GLPCIVGCLE ISISGREKRL VGPRGRVFYE GDVITVDGSN GDVLVGTAEM
LSPALDDGFQ TLLRWADNVR DIGIRANADT PEDARTARNF AADGIGLCRT EHMFFDEDRL
TVMREMIFAD ASQDRRLVLE RLLPMQRADF IALFDIMAGM PVCIRLFDPP LHEFLPHDRD
GMRDLADALD RPLSEVTRRI EAMSEFNPML GMRGVRLGVT IPEIYDMQAR AIFEAAVEAS
TRGAQVVPEI MIPLVSASRE VELVKSRIDA VAAAVRSETK AEFTYRLGAM METPRAALRA
GEIAEHAEFM SFGTNDLTQM TYGLSRDDAG RFMSTYVNQG VYAEDPFHIL DVEGVGELLL
IGAGRGRATR RDITISVCGE HGGNPESIAF CRAAGFDYVS CSPFRVPVAR LAAAHFALLA
PKSHG
//
