Reviewed, UniProtKB/Swiss-Prot Q05528 (KDUD_DICD3)

Names and origin

Protein names

Recommended name:
    2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
    EC=1.1.1.127
Alternative name(s):
    2-keto-3-deoxygluconate oxidoreductase
      Short name=KDG oxidoreductase
    2-keto-3-deoxygluconate 5-dehydrogenase

Gene names

Name:

kduD

Organism

Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))

Taxonomic identifier

198628 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH. Ref.1
Catalytic activity	2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH. Ref.1
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 5/5.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase activity Inferred from electronic annotation. Source: EC 2-deoxy-D-gluconate 3-dehydrogenase activity Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 253	253	2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase		PRO_0000054716
Regions
	Nucleotide binding	14 – 38	25	NAD By similarity
Sites
	Active site	158	1	Proton acceptor By similarity
	Binding site	145	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05528-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 59E9827DEA471F76	FASTA	253	27,275
	10 20 30 40 50 60 MILNTFNLQG KVALITGCDT GLGQGMAVGL AEAGCDIVGV NIVEPKETIE KVTAVGRRFL 70 80 90 100 110 120 SLTADMSDIS GHAALVEKAV AEFGKVDILV NNAGIIRRED AIEFSEKNWD DVMNLNIKSV 130 140 150 160 170 180 FFMSQTVARQ FIKQGHGGKI INIASMLSFQ GGIPVPSYTA SKKRVMGITR IVANEWAKHN 190 200 210 220 230 240 INVNAIAPGY MATNNTQHVR ADQDRSKEIL DRIPAGRWGL PQDLQGPAVF LASSASDYVN 250 GYTIAVDGGW LAR

References

[1]	"Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation." Condemine G., Robert-Baudouy J. Mol. Microbiol. 5:2191-2202(1991) [PubMed: 1766386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION IN PECTIN DEGRADATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62073 Genomic DNA. Translation: CAA43989.1.
PIR	S17711.
3D structure databases
HSSP	HSSP built from PDB template 1EDO based on UniProtKB Q93X62.
ModBase	Search...
Family and domain databases
InterPro	IPR011286. 2-deoxy-D-gluc_3_DH. IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
TIGRFAMs	TIGR01832. kduD. 1 hit.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KDUD_DICD3

Accession

Primary (citable) accession number: Q05528

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	September 22, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)