Q59470 (Q59470_KLEOX) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Diol dehydrase alpha subunit EMBL BAA08099.1
EC=4.2.1.28 EMBL BAA08099.1

Gene names

Name:

pddA EMBL BAA08099.1

Organism

Klebsiella oxytoca EMBL BAA08099.1

Taxonomic identifier

571 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Lyase EMBL BAA08099.1
Technical term	3D-structure PDB 1UC5 PDB 1IWB PDB 1EGV PDB 1EGM PDB 3AUJ PDB 1DIO PDB 1EEX PDB 1UC4
Gene Ontology (GO)
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: InterPro propanediol dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Site	143	1	Important for catalytic activity PDB 1DIO
	Site	170	1	Important for catalytic activity PDB 1DIO
	Site	296	1	Important for catalytic activity PDB 1DIO
	Site	335	1	Important for catalytic activity PDB 1DIO

Sequences

	Sequence		Length	Mass (Da)
	Q59470 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5AC48A035B65331D	FASTA	554	60,348
	10 20 30 40 50 60 MRSKRFEALA KRPVNQDGFV KEWIEEGFIA MESPNDPKPS IKIVNGAVTE LDGKPVSDFD 70 80 90 100 110 120 LIDHFIARYG INLNRAEEVM AMDSVKLANM LCDPNVKRSE IVPLTTAMTP AKIVEVVSHM 130 140 150 160 170 180 NVVEMMMAMQ KMRARRTPSQ QAHVTNVKDN PVQIAADAAE GAWRGFDEQE TTVAVARYAP 190 200 210 220 230 240 FNAIALLVGS QVGRPGVLTQ CSLEEATELK LGMLGHTCYA ETISVYGTEP VFTDGDDTPW 250 260 270 280 290 300 SKGFLASSYA SRGLKMRFTS GSGSEVQMGY AEGKSMLYLE ARCIYITKAA GVQGLQNGSV 310 320 330 340 350 360 SCIGVPSAVP SGIRAVLAEN LICSSLDLEC ASSNDQTFTH SDMRRTARLL MQFLPGTDFI 370 380 390 400 410 420 SSGYSAVPNY DNMFAGSNED AEDFDDYNVI QRDLKVDGGL RPVREEDVIA IRNKAARALQ 430 440 450 460 470 480 AVFAGMGLPP ITDEEVEAAT YAHGSKDMPE RNIVEDIKFA QEIINKNRNG LEVVKALAQG 490 500 510 520 530 540 GFTDVAQDML NIQKAKLTGD YLHTSAIIVG DGQVLSAVND VNDYAGPATG YRLQGERWEE 550 IKNIPGALDP NEID

References

[1]	"Molecular cloning, sequencing, and expression of the genes encoding adenosylcobalamin-dependent diol dehydrase of Klebsiella oxytoca." Tobimatsu T., Hara T., Sakaguchi M., Kishimoto Y., Wada Y., Isoda M., Sakai T., Toraya T. J. Biol. Chem. 270:7142-7148(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 8724 EMBL BAA08099.1.
[2]	"A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase." Shibata N., Masuda J., Tobimatsu T., Toraya T., Suto K., Morimoto Y., Yasuoka N. Structure 7:997-1008(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), ACTIVE SITE.
[3]	"How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex." Masuda J., Shibata N., Morimoto Y., Toraya T., Yasuoka N. Structure 8:775-788(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
[4]	"Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase." Shibata N., Masuda J., Morimoto Y., Yasuoka N., Toraya T. Biochemistry 41:12607-12617(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[5]	"Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase." Shibata N., Nakanishi Y., Fukuoka M., Yamanishi M., Yasuoka N., Toraya T. J. Biol. Chem. 278:22717-22725(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
[6]	"Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols." Yamanishi M., Kinoshita K., Fukuoka M., Saito T., Tanokuchi A., Ikeda Y., Obayashi H., Mori K., Shibata N., Tobimatsu T., Toraya T. FEBS J. 279:793-804(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D45071 Genomic DNA. Translation: BAA08099.1.

PIR

A56111.

RefSeq

YP_005016275.1. NC_016612.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DIO	X-ray	2.20	A/L	1-554	[»]
1EEX	X-ray	1.70	A/L	1-554	[»]
1EGM	X-ray	1.85	A/L	1-554	[»]
1EGV	X-ray	1.75	A/L	1-554	[»]
1IWB	X-ray	1.85	A/L	1-554	[»]
1UC4	X-ray	1.80	A/L	1-554	[»]
1UC5	X-ray	2.30	A/L	1-554	[»]
3AUJ	X-ray	2.10	A/L	1-554	[»]

ProteinModelPortal

Q59470.

SMR

Q59470. Positions 1-551.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q59470. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

11660425.

KEGG

kox:KOX_01455.

Phylogenomic databases

KO

K01699.

Family and domain databases

Gene3D

3.20.20.350. 1 hit.

InterPro

IPR016176. Cbl-dep_enz_cat.
IPR003206. Diol/glycerol_deHydtase_lsu.
[Graphical view]

Pfam

PF02286. Dehydratase_LU. 1 hit.
[Graphical view]

PIRSF

PIRSF018507. Prpndl_dhdrts_lg. 1 hit.

ProDom

PD025428. Diol/glycerol_deHydtase_lsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF51703. Cbl-dep_enz_cat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q59470.

Entry information

Entry name

Q59470_KLEOX

Accession

Primary (citable) accession number: Q59470

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)