ID A0A0G1TNI5_9BACT Unreviewed; 702 AA.
AC A0A0G1TNI5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=Pyruvate,orthophosphate dikinase {ECO:0000313|EMBL:KKU83386.1};
GN ORFNames=UY10_C0009G0004 {ECO:0000313|EMBL:KKU83386.1};
OS Microgenomates group bacterium GW2011_GWA2_47_8.
OC Bacteria.
OX NCBI_TaxID=1618503 {ECO:0000313|EMBL:KKU83386.1, ECO:0000313|Proteomes:UP000034016};
RN [1] {ECO:0000313|EMBL:KKU83386.1, ECO:0000313|Proteomes:UP000034016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU83386.1}.
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DR EMBL; LCOS01000009; KKU83386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1TNI5; -.
DR Proteomes; UP000034016; 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:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
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; 3.50.30.10; 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; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
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; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KKU83386.1};
KW Pyruvate {ECO:0000313|EMBL:KKU83386.1};
KW Transferase {ECO:0000313|EMBL:KKU83386.1}.
FT DOMAIN 1..71
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 210..293
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 702 AA; 75707 MW; 1289FF7C48DBDA26 CRC64;
MNPSAIQYRS MHGIPGEVGT AVTVQEMVFG NGTGQSGTAV IYTRHTDPAR HHEWEGYFMP
NAQGEQIVAG AESGALSVEV LPNNIRKQLS RHMATIEDIV GWVGDIEVTW ENGRLSFLQA
RKAKLPSYAT LAYAEAFHRE GRLELSEALS RIRPMDIEAV VRQSFDSEAK DQARASGRLL
TTGLPTSTGV ATGRLVFSVE AARSAVGRGE KVILLCEHFN PNDVDVIGGL GGLVTTTGTP
SSHIALVARA LNVPCIMGCL ETVPPGTGPS RTAIFSATAV EEGAMVSIDS AHGELFLGML
ALGKSQEIPS GIGALLEAWR ERNGTDNAWA MFVLSKDSRA REDMLRQCHE AIAKADHYDT
VKARDAAFIN HAFPTAISIP TAIVPLRGRD RDDVKRDVQT LVEALRRKGH GVWPRSAYGS
ISGGEPDALN SPYGSVDVGQ GDPDGARLTD WLTNPSSSVS KWGGLDSWYV FTDTAGEHTL
GELLIPADPP DKLAKPVVGE HFVFSLRATP EGIVVDMNDH TCHVRSLASI KQEDLMQIVA
HGGSDDASLV GSLTYRFGKH HLDSDKLTSL VGRLADTSGK DTVAKFKRKL ISVFGEGAVQ
STTTETLSSM VDTLGKQGLL GDADYALIMS DRSLEVAHAI RKTVFSDWWS AHALPLRMWA
IQHATGESQL ECQGRLSTDA KNNWMLIYGL KGGVESTIAI RR
//
