ID A0A0R2Q6R7_9ACTN Unreviewed; 661 AA.
AC A0A0R2Q6R7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
DE Flags: Fragment;
GN ORFNames=ABR56_03000 {ECO:0000313|EMBL:KRO45854.1};
OS Acidimicrobium sp. BACL27 MAG-120823-bin4.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=1655564 {ECO:0000313|EMBL:KRO45854.1, ECO:0000313|Proteomes:UP000050870};
RN [1] {ECO:0000313|EMBL:KRO45854.1, ECO:0000313|Proteomes:UP000050870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL17 MAG-120823-bin4 {ECO:0000313|EMBL:KRO45854.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO45854.1}.
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DR EMBL; LIAO01000289; KRO45854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2Q6R7; -.
DR Proteomes; UP000050870; 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; 3.30.1490.20; ATP-grasp fold, A domain; 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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
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; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KRO45854.1};
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:KRO45854.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRO45854.1}.
FT DOMAIN 1..87
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 97..144
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 219..298
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 316..659
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRO45854.1"
FT NON_TER 661
FT /evidence="ECO:0000313|EMBL:KRO45854.1"
SQ SEQUENCE 661 AA; 71866 MW; D30C8A382B394A9A CRC64;
AVEAVFRSWN GARAIAYRVR EKISHDLGTA VNVQAMVFGN RDNNSGTGVG FTRNAATGEN
KPYGDYLINA QGEDVVAGIR NTEDLDALKR QFPSVHKELL AIFDRLERHY HDMCDTEFTI
DQGKLWMLQT RVGKRTGAAA LKMAVDMTAG TGKGKQSWKI TKKEALMRVN AEHLDQVLHP
QFTNKTKAVA KGLAASPGAA VGKVYFTADD AEAAAKSGEA VILVRSETSP EDVHGMMVAK
GILTSRGGLV SHAAVVARGW GTPAVVGADA VQIDGKMFRA GDVVVREGDV ISLDGTTGEV
MLGAMQLTAA EPTKEFQTIL KWADEFRKGK LAVRANADTA EDALKAREYG AEGIGLCRTE
HMFLAPDRLP VVRRMILAST PAEEMAALED LRAVQKEDFA SLLRAMSGLP VTVRLLDPPL
HEFLPNVDEL EIKAATSGLD EQERKLLRAA HDWAEVNPML GTRGVRLGVI KPGLYAMQVR
ALMQAADQVA DEGYEPIVEV MIPLTVTREE LALARSWVEG VLVEHSSRLK DKGAGLGKRG
ARGKKITRPK VTIGTMIETP RAALRADELA EHADFFSFGT NDLTQMTFGF SRDDVESRMM
PAYLEAGLLK RNPFETIDQT GVGELVEIAA KRGRKAKRKL KLGVCGEHGG DPESIALFYR
A
//
