ID O33199_MYCTO Unreviewed; 207 AA. AC O33199; F2GK38; Q7D845; DT 01-JAN-1998, integrated into UniProtKB/TrEMBL. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 152. DE SubName: Full=MutT/nudix family protein {ECO:0000313|EMBL:AAK46008.1}; GN OrderedLocusNames=MT1739 {ECO:0000313|EMBL:AAK46008.1}; OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK46008.1, ECO:0000313|Proteomes:UP000001020}; RN [1] {ECO:0000313|EMBL:AAK46008.1, ECO:0000313|Proteomes:UP000001020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020}; RX PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J., DeBoy R., Dodson R., Gwinn M., Haft D., Hickey E., RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M., Salzberg S.L., RA Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A., RA Bishai W., Jacobs Jr W.R.Jr., Venter J.C., Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). RN [2] {ECO:0007829|PDB:1MK1, ECO:0007829|PDB:1MP2} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND ACTIVE SITE. RX PubMed=12906832; DOI=10.1016/s0969-2126(03)00154-0; RA Kang L.W., Gabelli S.B., Cunningham J.E., O'Handley S.F., Amzel L.M.; RT "Structure and mechanism of MT-ADPRase, a nudix hydrolase from RT Mycobacterium tuberculosis."; RL Structure 11:1015-1023(2003). 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; AE000516; AAK46008.1; -; Genomic_DNA. DR PIR; C70503; C70503. DR RefSeq; WP_003408399.1; NZ_KK341227.1. DR PDB; 1MK1; X-ray; 2.00 A; A=1-207. DR PDB; 1MP2; X-ray; 2.30 A; A=1-207. DR PDB; 1MQE; X-ray; 2.00 A; A=1-207. DR PDB; 1MQW; X-ray; 2.30 A; A=1-207. DR PDB; 1MR2; X-ray; 2.30 A; A=1-207. DR PDBsum; 1MK1; -. DR PDBsum; 1MP2; -. DR PDBsum; 1MQE; -. DR PDBsum; 1MQW; -. DR PDBsum; 1MR2; -. DR AlphaFoldDB; O33199; -. DR SMR; O33199; -. DR DrugBank; DB03148; Adenosine 5'-methylenediphosphate. DR DrugBank; DB02059; Adenosine-5-Diphosphoribose. DR DrugBank; DB01975; AMPCPR. DR GeneID; 45425669; -. DR KEGG; mtc:MT1739; -. DR PATRIC; fig|83331.31.peg.1867; -. DR HOGENOM; CLU_062658_5_0_11; -. DR BRENDA; 3.6.1.13; 3445. DR EvolutionaryTrace; O33199; -. DR Proteomes; UP000001020; Chromosome. DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE. DR CDD; cd03424; ADPRase_NUDT5; 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1. DR PANTHER; PTHR11839:SF15; URIDINE DIPHOSPHATE GLUCOSE PYROPHOSPHATASE NUDT14; 1. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; Nudix; 1. DR PROSITE; PS51462; NUDIX; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1MK1, ECO:0007829|PDB:1MP2}; KW Metal-binding {ECO:0007829|PDB:1MQW, ECO:0007829|PDB:1MR2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001020}. FT DOMAIN 41..172 FT /note="Nudix hydrolase" FT /evidence="ECO:0000259|PROSITE:PS51462" FT ACT_SITE 142 FT /note="EMO_00116 metal ligand,EMO_00066 proton acceptor" FT /evidence="ECO:0007829|PDB:1MQW" FT BINDING 76 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MR2" FT BINDING 76 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MQW" FT BINDING 93 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MR2" FT BINDING 93 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MQW" FT BINDING 97 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MQW" FT BINDING 97 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MR2" FT BINDING 97 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MQW" FT BINDING 142 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MQW" FT BINDING 142 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MQW" FT SITE 64 FT /note="EMO_00033 electrostatic stabiliser" FT /evidence="ECO:0007829|PDB:1MQW" FT SITE 76 FT /note="EMO_00116 metal ligand" FT /evidence="ECO:0007829|PDB:1MQW" FT SITE 93 FT /note="EMO_00116 metal ligand" FT /evidence="ECO:0007829|PDB:1MQW" FT SITE 97 FT /note="EMO_00116 metal ligand" FT /evidence="ECO:0007829|PDB:1MQW" SQ SEQUENCE 207 AA; 22893 MW; 7FB78C9C984FA85E CRC64; MAEHDFETIS SETLHTGAIF ALRRDQVRMP GGGIVTREVV EHFGAVAIVA MDDNGNIPMV YQYRHTYGRR LWELPAGLLD VAGEPPHLTA ARELREEVGL QASTWQVLVD LDTAPGFSDE SVRVYLATGL REVGRPEAHH EEADMTMGWY PIAEAARRVL RGEIVNSIAI AGVLAVHAVT TGFAQPRPLD TEWIDRPTAF AARRAER //