ID A3DJ38_ACET2 Unreviewed; 870 AA. AC A3DJ38; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 116. DE SubName: Full=Metallophosphoesterase {ECO:0000313|EMBL:ABN53967.1}; GN OrderedLocusNames=Cthe_2768 {ECO:0000313|EMBL:ABN53967.1}; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN53967.1, ECO:0000313|Proteomes:UP000002145}; RN [1] {ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:3TY5, ECO:0007829|PDB:3TY8} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 479-870 IN COMPLEX WITH ADP; AMP; RP ATP AND MAGNESIUM. RX PubMed=22308407; DOI=10.1073/pnas.1116827109; RA Smith P., Wang L.K., Nair P.A., Shuman S.; RT "The adenylyltransferase domain of bacterial Pnkp defines a unique RNA RT ligase family."; RL Proc. Natl. Acad. Sci. U.S.A. 109:2296-2301(2012). RN [3] {ECO:0007829|PDB:4DRF, ECO:0007829|PDB:4E6N} RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 445-870 IN COMPLEX WITH AMP. RX PubMed=22847431; DOI=10.1073/pnas.1209805109; RA Wang P., Chan C.M., Christensen D., Zhang C., Selvadurai K., Huang R.H.; RT "Molecular basis of bacterial protein Hen1 activating the ligase activity RT of bacterial protein Pnkp for RNA repair."; RL Proc. Natl. Acad. Sci. U.S.A. 109:13248-13253(2012). RN [4] {ECO:0007829|PDB:4GP6, ECO:0007829|PDB:4GP7} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-170 IN COMPLEX WITH ADP AND RP ATP. RX PubMed=23118415; DOI=10.1261/rna.036061.112; RA Wang L.K., Das U., Smith P., Shuman S.; RT "Structure and mechanism of the polynucleotide kinase component of the RT bacterial Pnkp-Hen1 RNA repair system."; RL RNA 18:2277-2286(2012). RN [5] {ECO:0007829|PDB:4JST, ECO:0007829|PDB:4JSY} RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-170 IN COMPLEX WITH CTP AND RP GTP. RX PubMed=23721485; DOI=10.1021/bi400412x; RA Das U., Wang L.K., Smith P., Shuman S.; RT "Structural and biochemical analysis of the phosphate donor specificity of RT the polynucleotide kinase component of the bacterial pnkphen1 RNA repair RT system."; RL Biochemistry 52:4734-4743(2013). RN [6] {ECO:0000313|EMBL:ABN53967.1, ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RX PubMed=24295562; DOI=10.1186/1754-6834-6-179; RA Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M., RA Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H., RA Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.; RT "Global transcriptome analysis of Clostridium thermocellum ATCC 27405 RT during growth on dilute acid pretreated Populus and switchgrass."; RL Biotechnol. Biofuels 6:179-179(2013). RN [7] {ECO:0007829|PDB:4J6O} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 171-424 IN COMPLEX WITH RP MANGANESE. RX PubMed=23595150; DOI=10.1093/nar/gkt221; RA Wang L.K., Smith P., Shuman S.; RT "Structure and mechanism of the 2',3' phosphatase component of the RT bacterial Pnkp-Hen1 RNA repair system."; RL Nucleic Acids Res. 41:5864-5873(2013). RN [8] {ECO:0007829|PDB:4QM6, ECO:0007829|PDB:4QM7} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-170 IN COMPLEX WITH GTP AND RP MG(2+). RX PubMed=25266383; DOI=10.1128/JB.02197-14; RA Das U., Wang L.K., Smith P., Munir A., Shuman S.; RT "Structures of bacterial polynucleotide kinase in a michaelis complex with RT nucleoside triphosphate (NTP)-Mg2+ and 5'-OH RNA and a mixed substrate- RT product complex with NTP-Mg2+ and a 5'-phosphorylated oligonucleotide."; RL J. Bacteriol. 196:4285-4292(2014). RN [9] {ECO:0007829|PDB:4MDE, ECO:0007829|PDB:4MDF} RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-170 IN COMPLEX WITH GTP. RX PubMed=24150947; DOI=10.1093/nar/gkt936; RA Das U., Wang L.K., Smith P., Jacewicz A., Shuman S.; RT "Structures of bacterial polynucleotide kinase in a Michaelis complex with RT GTPMg2+ and 5'-OH oligonucleotide and a product complex with GDPMg2+ and RT 5'-PO4 oligonucleotide reveal a mechanism of general acid-base catalysis RT and the determinants of phosphoacceptor recognition."; RL Nucleic Acids Res. 42:1152-1161(2014). CC -!- INTERACTION: CC A3DJ38; A3DJ37: Cthe_2767; NbExp=2; IntAct=EBI-16002232, EBI-16002195; 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; CP000568; ABN53967.1; -; Genomic_DNA. DR RefSeq; WP_020457916.1; NC_009012.1. DR PDB; 3TY5; X-ray; 2.40 A; A/B=479-870. DR PDB; 3TY8; X-ray; 2.60 A; A/B=479-870. DR PDB; 3TY9; X-ray; 3.12 A; A/B/C/D=479-870. DR PDB; 4DRF; X-ray; 2.60 A; A/C=445-870. DR PDB; 4E6N; X-ray; 2.39 A; A/C=445-870. DR PDB; 4GP6; X-ray; 2.10 A; A/B=1-170. DR PDB; 4GP7; X-ray; 2.00 A; A/B=1-170. DR PDB; 4J6O; X-ray; 1.60 A; A/B=171-424. DR PDB; 4JST; X-ray; 2.03 A; A/B=1-170. DR PDB; 4JSY; X-ray; 2.14 A; A/B=1-170. DR PDB; 4JT2; X-ray; 2.49 A; A/B=1-170. DR PDB; 4JT4; X-ray; 2.01 A; A/B=1-170. DR PDB; 4MDE; X-ray; 1.80 A; A/B=1-170. DR PDB; 4MDF; X-ray; 1.73 A; A/B=1-170. DR PDB; 4QM6; X-ray; 1.50 A; A/B=1-170. DR PDB; 4QM7; X-ray; 1.80 A; A/B=1-170. DR PDBsum; 3TY5; -. DR PDBsum; 3TY8; -. DR PDBsum; 3TY9; -. DR PDBsum; 4DRF; -. DR PDBsum; 4E6N; -. DR PDBsum; 4GP6; -. DR PDBsum; 4GP7; -. DR PDBsum; 4J6O; -. DR PDBsum; 4JST; -. DR PDBsum; 4JSY; -. DR PDBsum; 4JT2; -. DR PDBsum; 4JT4; -. DR PDBsum; 4MDE; -. DR PDBsum; 4MDF; -. DR PDBsum; 4QM6; -. DR PDBsum; 4QM7; -. DR AlphaFoldDB; A3DJ38; -. DR SMR; A3DJ38; -. DR DIP; DIP-60067N; -. DR IntAct; A3DJ38; 1. DR STRING; 203119.Cthe_2768; -. DR KEGG; cth:Cthe_2768; -. DR eggNOG; COG0639; Bacteria. DR eggNOG; COG4639; Bacteria. DR HOGENOM; CLU_016728_0_0_9; -. DR OrthoDB; 9779903at2; -. DR BRENDA; 2.7.1.78; 1530. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd07423; MPP_Prp_like; 1. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR041780; MPP_PrpE-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR024028; PNKP_bac. DR InterPro; IPR032380; PNKP_ligase_dom. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR NCBIfam; TIGR04075; bacter_Pnkp; 1. DR PANTHER; PTHR42850:SF7; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE PRPE [ASYMMETRICAL]; 1. DR PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 1. DR Pfam; PF13671; AAA_33; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16542; PNKP_ligase; 1. DR PRINTS; PR00114; STPHPHTASE. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3TY5, ECO:0007829|PDB:3TY8}; KW ATP-binding {ECO:0007829|PDB:3TY5, ECO:0007829|PDB:4GP7}; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW GTP-binding {ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4GP6}; KW Nucleotide-binding {ECO:0007829|PDB:3TY5, ECO:0007829|PDB:3TY9}; KW Reference proteome {ECO:0000313|Proteomes:UP000002145}. FT DOMAIN 181..379 FT /note="Calcineurin-like phosphoesterase" FT /evidence="ECO:0000259|Pfam:PF00149" FT DOMAIN 474..865 FT /note="Polynucleotide kinase-phosphatase ligase" FT /evidence="ECO:0000259|Pfam:PF16542" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 17 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 17 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 17 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 18 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 18 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 18 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 18 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 18 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 19 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 19 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 19 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 20 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 20 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 20 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 20 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 20 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 21 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 21 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 21 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 21 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 21 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 22 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 22 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 22 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6, ECO:0007829|PDB:4JT4" FT BINDING 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4GP7, ECO:0007829|PDB:4JST" FT BINDING 22 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 22 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 23 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 23 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 23 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 23 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 23 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4GP7, ECO:0007829|PDB:4JST" FT BINDING 120 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP6" FT BINDING 120 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 120 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 120 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4MDE" FT BINDING 120 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 120 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 120 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4GP7" FT BINDING 123 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0007829|PDB:4JT2" FT BINDING 123 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007829|PDB:4JSY, ECO:0007829|PDB:4MDF" FT BINDING 123 FT /ligand="UTP" FT /ligand_id="ChEBI:CHEBI:46398" FT /evidence="ECO:0007829|PDB:4JST" FT BINDING 123 FT /ligand="dATP" FT /ligand_id="ChEBI:CHEBI:61404" FT /evidence="ECO:0007829|PDB:4JT4" FT BINDING 187 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:4J6O" FT BINDING 189 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:4J6O" FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:4J6O" FT BINDING 495 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 496 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 529 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 530 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 531 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:3TY9" FT BINDING 531 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 532 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 536 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 536 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 536 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 565 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 565 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 607 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 607 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 639 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 687 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9" FT BINDING 734 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3TY9" FT BINDING 737 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3TY9" FT BINDING 774 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 774 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 774 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 792 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 792 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9, ECO:0007829|PDB:4E6N" FT BINDING 792 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" FT BINDING 794 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:3TY9" FT BINDING 824 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3TY5" SQ SEQUENCE 870 AA; 98776 MW; 11CA5878DD2919E9 CRC64; MKLTIPELSL VVLIGSSGSG KSTFAKKHFK PTEVISSDFC RGLVSDDEND QTVTGAAFDV LHYIVSKRLQ LGKLTVVDAT NVQESARKPL IEIAKDYHCF PVAVVFNLPE KVCQERNKNR TDRQVEEYVI RKHTQQLKKS IKGLQREGFR YVYILNSPEE VEEVVFERQP LWNNKKDEHG PFDIIGDIHG CYDELKMLLE KLGYLIEEVE GGVGSGKYRV THPEGRKVLF LGDLVDRGPK ITEVLKLVMG MVKSGIALCV PGNHDVKLLR KLNGRDVQIT HGLDRTLEQL AKEPQEFIEE VKAFIDGLVS HYVLDDGKLV VAHAGMKEEF QGRGSGKVRE FALYGETTGE TDEYGLPVRY DWASDYRGKA LVVYGHTPQA EVLKVNNTIN IDTGCVFGGK LTAYRYPERE IVDVKALKTY YEPAKPFLPK EDMAERFEAR TDNDILDIND VLGKKIITTR LMSSITIHEE NSIAALEVMS RFAADPHWLI YLPPTMSPCE TSKKEGMLEH PIEAFEYFRT RGVGKVVCEQ KHMGSRAVVI VCKDSQVAEK RFGVLDGTAG ICYTRTGRHF FDDMQLEAEL IDRVRKVLDK SGFWGDFNTD WVCLDCELMP WSAKAQKLLE EQYSAVGISG RVVLDEAVKL LKQASLNKTV SFDVSRQTSG KNADINELLQ RFTERSEMMQ KYVEAYRKYC WPVNSIDDLK LAPFHILATE GKVHSDKNHI WHMDTIAKYC TQDDSLIMAT NHILVDVTDA ESVDKGIKWW EDLTASGGEG MVVKPYDFIV KNGRELLQPA VKCRGREYLR IIYGPEYTMD ENIERLRNRA VGKKRSLALR EFSLGMEALE RFVRNEPLYR VHECVFGVLA LESEPVDPRL //