Q0T9J7 (ULAD_ECOL5) 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:	ECP_4441

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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 MF_01267
Catalytic activity	3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO2. HAMAP MF_01267
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01267
Pathway	Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 2/4. HAMAP MF_01267
Subunit structure	Homodimer By similarity. HAMAP MF_01267
Induction	Induced by L-ascorbate. Repressed by ulaR By similarity. HAMAP 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 base biosynthetic process Inferred from electronic annotation. Source: InterPro L-ascorbic acid catabolic process Inferred from electronic annotation. Source: InterPro carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-dehydro-L-gulonate-6-phosphate decarboxylase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro 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 MF_01267		PRO_1000067320
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)
	Q0T9J7 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: EC8490DA1D02D824	FASTA	216	23,578
	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 GQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF 190 200 210 KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 536 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000247 Genomic DNA. Translation: ABG72382.1.
RefSeq	YP_672283.1. NC_008253.1.
3D structure databases
ProteinModelPortal	Q0T9J7.
SMR	Q0T9J7. Positions 2-216.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0T9J7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000045814; EBESCP00000044003; EBESCG00000044864.
GeneID	4190033.
GenomeReviews	Gene locus ECP_4441 in contig CP000247_GR.
KEGG	ecp:ECP_4441.
PATRIC	18199822. VBIEscCol77757_4487.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0269.
GeneTree	EBGT00050000008924.
HOGENOM	HBG417610.
OMA	PIYIFIA.
PhylomeDB	Q0T9J7.
ProtClustDB	PRK13306.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_4441-MONOMER.
Family and domain databases
HAMAP	MF_01267. UlaD. [Tree]
InterPro	IPR023942. 3-keto-L-gulonate6Pdecase_UlaD. IPR013785. Aldolase_TIM. IPR001754. OMPdeCOase_dom. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K03078.
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_ECOL5

Accession

Primary (citable) accession number: Q0T9J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program