ID Q59471_KLEOX Unreviewed; 224 AA. AC Q59471; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 122. DE SubName: Full=Diol dehydrase beta subunit {ECO:0000313|EMBL:BAA08100.1}; DE EC=4.2.1.28 {ECO:0000313|EMBL:BAA08100.1}; GN Name=pddB {ECO:0000313|EMBL:BAA08100.1}; OS Klebsiella oxytoca. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=571 {ECO:0000313|EMBL:BAA08100.1}; RN [1] {ECO:0000313|EMBL:BAA08100.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 8724 {ECO:0000313|EMBL:BAA08100.1}; RX PubMed=7706251; DOI=10.1074/jbc.270.13.7142; RA Tobimatsu T., Hara T., Sakaguchi M., Kishimoto Y., Wada Y., Isoda M., RA Sakai T., Toraya T.; RT "Molecular cloning, sequencing, and expression of the genes encoding RT adenosylcobalamin-dependent diol dehydrase of Klebsiella oxytoca."; RL J. Biol. Chem. 270:7142-7148(1995). RN [2] {ECO:0007829|PDB:1DIO} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COB(II)ALAMIN. RX PubMed=10467140; DOI=10.1016/s0969-2126(99)80126-9; RA Shibata N., Masuda J., Tobimatsu T., Toraya T., Suto K., Morimoto Y., RA Yasuoka N.; RT "A new mode of B12 binding and the direct participation of a potassium ion RT in enzyme catalysis: X-ray structure of diol dehydratase."; RL Structure 7:997-1008(1999). RN [3] {ECO:0007829|PDB:1EEX, ECO:0007829|PDB:1EGM} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CYANOCOB(III)ALAMIN. RX PubMed=10903944; DOI=10.1016/s0969-2126(00)00164-7; RA Masuda J., Shibata N., Morimoto Y., Toraya T., Yasuoka N.; RT "How a protein generates a catalytic radical from coenzyme B(12): X-ray RT structure of a diol-dehydratase-adeninylpentylcobalamin complex."; RL Structure 8:775-788(2000). RN [4] {ECO:0007829|PDB:1IWB} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH COB(II)ALAMIN. RX PubMed=12379103; DOI=10.1021/bi026104z; RA Shibata N., Masuda J., Morimoto Y., Yasuoka N., Toraya T.; RT "Substrate-induced conformational change of a coenzyme B12-dependent RT enzyme: crystal structure of the substrate-free form of diol dehydratase."; RL Biochemistry 41:12607-12617(2002). RN [5] {ECO:0007829|PDB:1UC4, ECO:0007829|PDB:1UC5} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH CYANOCOB(III)ALAMIN. RX PubMed=12684496; DOI=10.1074/jbc.m301513200; RA Shibata N., Nakanishi Y., Fukuoka M., Yamanishi M., Yasuoka N., Toraya T.; RT "Structural rationalization for the lack of stereospecificity in coenzyme RT B12-dependent diol dehydratase."; RL J. Biol. Chem. 278:22717-22725(2003). RN [6] {ECO:0007829|PDB:3AUJ} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH CA(2+). RX PubMed=22221669; DOI=10.1111/j.1742-4658.2012.08470.x; RA Yamanishi M., Kinoshita K., Fukuoka M., Saito T., Tanokuchi A., Ikeda Y., RA Obayashi H., Mori K., Shibata N., Tobimatsu T., Toraya T.; RT "Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to RT the mechanism-based inactivation by glycerol and act on longer chain 1,2- RT diols."; RL FEBS J. 279:793-804(2012). RN [7] {ECO:0007829|PDB:5YRT, ECO:0007829|PDB:5YRV} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 46-224 IN COMPLEX WITH RP COB(II)ALAMIN. RX PubMed=29797764; DOI=10.1002/anie.201803591; RA Shibata N., Sueyoshi Y., Higuchi Y., Toraya T.; RT "Direct Participation of a Peripheral Side Chain of a Corrin Ring in RT CoenzymeB12 Catalysis."; RL Angew. Chem. Int. Ed. 57:7830-7835(2018). RN [8] {ECO:0007829|PDB:7XRK, ECO:0007829|PDB:7XRL} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 46-224 IN COMPLEX WITH RP COB(II)ALAMIN. RX PubMed=35974426; DOI=10.1002/chem.202202196; RA Shibata N., Higuchi Y., Krautler B., Toraya T.; RT "Structural Insights into the Very Low Activity of the Homocoenzyme RT B12 Adenosylmethylcobalamin in Coenzyme B12 RT -Dependent Diol Dehydratase and Ethanolamine Ammonia-Lyase."; RL Chemistry 28:e202202196-e202202196(2022). 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; D45071; BAA08100.1; -; Genomic_DNA. DR PIR; B56111; B56111. DR PDB; 1DIO; X-ray; 2.20 A; B/E=1-224. DR PDB; 1EEX; X-ray; 1.70 A; B/E=1-224. DR PDB; 1EGM; X-ray; 1.85 A; B/E=1-224. DR PDB; 1EGV; X-ray; 1.75 A; B/E=1-224. DR PDB; 1IWB; X-ray; 1.85 A; B/E=1-224. DR PDB; 1UC4; X-ray; 1.80 A; B/E=1-224. DR PDB; 1UC5; X-ray; 2.30 A; B/E=1-224. DR PDB; 3AUJ; X-ray; 2.10 A; B/E=1-224. DR PDB; 5YRT; X-ray; 1.70 A; B/E/H/K=46-224. DR PDB; 5YRV; X-ray; 1.55 A; B/E/H/K=46-224. DR PDB; 5YSH; X-ray; 1.90 A; B/E/H/K=46-224. DR PDB; 7XRK; X-ray; 2.30 A; B/E=46-224. DR PDB; 7XRL; X-ray; 1.75 A; B/E=46-224. DR PDBsum; 1DIO; -. DR PDBsum; 1EEX; -. DR PDBsum; 1EGM; -. DR PDBsum; 1EGV; -. DR PDBsum; 1IWB; -. DR PDBsum; 1UC4; -. DR PDBsum; 1UC5; -. DR PDBsum; 3AUJ; -. DR PDBsum; 5YRT; -. DR PDBsum; 5YRV; -. DR PDBsum; 5YSH; -. DR AlphaFoldDB; Q59471; -. DR SMR; Q59471; -. DR IntAct; Q59471; 2. DR MINT; Q59471; -. DR BRENDA; 4.2.1.28; 2811. DR EvolutionaryTrace; Q59471; -. DR GO; GO:0050215; F:propanediol dehydratase activity; IEA:UniProtKB-EC. DR DisProt; DP01028; -. DR Gene3D; 3.40.50.10150; B12-dependent dehydatase associated subunit; 1. DR InterPro; IPR010254; B12-dep_deHydtase_bsu. DR InterPro; IPR003208; Dehydtase/Dehydtase_re. DR InterPro; IPR025541; Ppandiol/glycerol_DHydtase_msu. DR Pfam; PF02288; Dehydratase_MU; 1. DR PIRSF; PIRSF018506; Prpndl_dhdrts_md; 1. DR SUPFAM; SSF52968; B12-dependent dehydatase associated subunit; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1EEX}; KW Lyase {ECO:0000313|EMBL:BAA08100.1}. FT BINDING 112 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 112 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 135 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:7XRL" FT BINDING 135 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 137 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 137 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 150 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 150 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 155 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 155 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 156 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 156 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 157 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 157 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" FT BINDING 197 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:7XRK, ECO:0007829|PDB:7XRL" FT BINDING 200 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0007829|PDB:1DIO, ECO:0007829|PDB:1IWB" FT BINDING 200 FT /ligand="cyanocob(III)alamin" FT /ligand_id="ChEBI:CHEBI:17439" FT /evidence="ECO:0007829|PDB:1EGM, ECO:0007829|PDB:1UC4" SQ SEQUENCE 224 AA; 24114 MW; C0A7C45A55CFAC7D CRC64; MEINEKLLRQ IIEDVLSEMK GSDKPVSFNA PAASAAPQAT PPAGDGFLTE VGEARQGTQQ DEVIIAVGPA FGLAQTVNIV GIPHKSILRE VIAGIEEEGI KARVIRCFKS SDVAFVAVEG NRLSGSGISI GIQSKGTTVI HQQGLPPLSN LELFPQAPLL TLETYRQIGK NAARYAKRES PQPVPTLNDQ MARPKYQAKS AILHIKETKY VVTGKNPQEL RVAL //