B7LCQ5 (ULAD_ECO55) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-keto-L-gulonate-6-phosphate decarboxylase UlaD
EC=4.1.1.85

Alternative name(s):
3-dehydro-L-gulonate-6-phosphate decarboxylase
KGPDC
L-ascorbate utilization protein D

Gene names

Name:	ulaD
Ordered Locus Names:	EC55989_4753

Organism

Escherichia coli (strain 55989 / EAEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585055 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization By similarity. HAMAP-Rule MF_01267
Catalytic activity	3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO2. HAMAP-Rule MF_01267
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 2/4. HAMAP-Rule MF_01267
Subunit structure	Homodimer By similarity.
Induction	Induced by L-ascorbate. Repressed by UlaR By similarity. HAMAP-Rule MF_01267
Sequence similarities	Belongs to the HPS/KGPDC family. KGPDC subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Magnesium Metal-binding
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	'de novo' pyrimidine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro L-ascorbic acid catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	3-dehydro-L-gulonate-6-phosphate decarboxylase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: HAMAP orotidine-5'-phosphate decarboxylase activity 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 – 216	216	3-keto-L-gulonate-6-phosphate decarboxylase UlaD HAMAP-Rule MF_01267		PRO_1000165141
Sites
	Metal binding	33	1	Magnesium By similarity
	Metal binding	62	1	Magnesium By similarity
	Binding site	11	1	Substrate By similarity
	Binding site	192	1	Substrate By similarity
	Site	64	1	Transition state stabilizer By similarity
	Site	67	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7LCQ5 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: CDF287AC1D1BAD68	FASTA	216	23,649
	10 20 30 40 50 60 MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL 70 80 90 100 110 120 ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE 130 140 150 160 170 180 QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF 190 200 210 KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 55989 / EAEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928145 Genomic DNA. Translation: CAV01690.1.
RefSeq	YP_002405613.1. NC_011748.1.
3D structure databases
ProteinModelPortal	B7LCQ5.
SMR	B7LCQ5. Positions 2-216.
ModBase	Search...
Protein-protein interaction databases
STRING	585055.EC55989_4753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAV01690; CAV01690; EC55989_4753.
GeneID	7147915.
KEGG	eck:EC55989_4753.
PATRIC	38483098. VBIEscCol113220_4776.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0269.
HOGENOM	HOG000226068.
KO	K03078.
OMA	IFIAGRS.
ProtClustDB	PRK13306.
Enzyme and pathway databases
BioCyc	ECOL585055:GJOM-4826-MONOMER.
UniPathway	UPA00263; UER00378.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01267. UlaD.
InterPro	IPR023942. 3-keto-L-gulonate6Pdecase_UlaD. IPR013785. Aldolase_TIM. IPR001754. OMPdeCOase_dom. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Pfam	PF00215. OMPdecase. 1 hit. [Graphical view]
SMART	SM00934. OMPdecase. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ULAD_ECO55

Accession

Primary (citable) accession number: B7LCQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program