ID A0JS53_ARTS2 Unreviewed; 906 AA.
AC A0JS53;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:ABK01873.1};
DE EC=2.7.9.2 {ECO:0000313|EMBL:ABK01873.1};
GN OrderedLocusNames=Arth_0474 {ECO:0000313|EMBL:ABK01873.1};
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK01873.1, ECO:0000313|Proteomes:UP000000754};
RN [1] {ECO:0000313|Proteomes:UP000000754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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DR EMBL; CP000454; ABK01873.1; -; Genomic_DNA.
DR RefSeq; WP_011690342.1; NC_008541.1.
DR AlphaFoldDB; A0JS53; -.
DR STRING; 290399.Arth_0474; -.
DR KEGG; art:Arth_0474; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_11; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000000754; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 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 PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABK01873.1};
KW Pyruvate {ECO:0000313|EMBL:ABK01873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000754};
KW Transferase {ECO:0000313|EMBL:ABK01873.1}.
FT DOMAIN 31..261
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 269..316
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 831..902
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 95829 MW; DC3F4D0565B628CA CRC64;
MAHVSPAPAP ASGAGNSLVV DLAELASGSL ALVGGKALNL GKLAAAGFPV PAGFCLTTTG
YRMAAPAELD YIAARLDGAN GLDGAKKYDG APGLPDDQRD GLARQAREAM AAAQVPADVE
AAVRGAYAAM GDAPVAVRSS ATAEDLPFAS FAGQQDSFMD VIGADAVVQA VRRCWASLWT
DRAVAYRTAN GISNREAGLA VVVQQMVDAG TAGVLFTANP VTGTRTESVI DSSPGPGQAV
VSGAVNPDHF VVDTATSRIL QGPQGAGTSL DPAQVRELTS LGDAAQRLFG APQDVEWVID
AGGKAWLTQS RPITTLYPLP EDESPGGTGG ADRTAGGDTR VYLCGTLLQG LTRPLTPMGL
SVLGLMRNSK GPWKYVNPGL RMYVDLTAVV RNKSGRKALL RLLPLADGRS AAVFPALLED
PRFSIVRPAR RLPGRKRTKG HAGTEAKGTE ESQSLVLMAG LIPAMIRALL WPDGELRRAR
RYQDRLEARL ALPLPANPAR RLQHAEDVLG STVNGIIQAT LPGPSVGYLM LAAARRLLRG
IAKPRELEAV LRGLPHNVTT IMDLELWQLA VSLGRDPESR RVFTELRPDG LAALYTAGGL
PSVAQAGLRT FLSKYGHRAV AEIDLGMPRW AEEPDHLLGI ISNYLRVEDP EQAPDRQFAR
AADHAEARVS ELVERAAARS RLRGRLVALC LRRARQLSGL RELPKFYIVM VLAEMHRQLT
AVGEELTRTG NISAATDVFF LDFEELRVAL RGADLKEVVA VRRRMYDVEL RRRRVPRLLL
SDGTDVEAAM MAAAAALPQA AAADRLTGTP ASAGTATGKV RVIMDPVGAH VEPGEILVAP
STDPGWTPLF LTAGALVMEM GGVISHGAVV AREYGIPAVV GVADATVRLR DGQTVTVDGA
AGTVTW
//