Reviewed, UniProtKB/Swiss-Prot Q0TAG1 (RHAD_ECOL5)

Names and origin

Protein names

Recommended name:
    Rhamnulose-1-phosphate aldolase
    EC=4.1.2.19

Gene names

Name:	rhaD
Ordered Locus Names:	ECP_4112

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	274 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde By similarity.
Catalytic activity	L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. HAMAP MF_00770
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 3/3. HAMAP MF_00770
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the aldolase class II family. RhaD subfamily.

Ontologies

Keywords
Biological process	Rhamnose metabolism
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	rhamnose metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	rhamnulose-1-phosphate aldolase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 274	274	Rhamnulose-1-phosphate aldolase HAMAP MF_00770		PRO_1000017338
Sites
	Active site	117	1	By similarity
	Metal binding	141	1	Zinc By similarity
	Metal binding	143	1	Zinc By similarity
	Metal binding	212	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0TAG1-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 3AFF0BE156FBAC06	FASTA	274	30,159
	10 20 30 40 50 60 MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ 70 80 90 100 110 120 PMPLLANTPF IVTGSGKFFR NVQLDPAANL GIVKVDSDGA GYHILWGLTN EAVPTSELPA 130 140 150 160 170 180 HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV 190 200 210 220 230 240 GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGPT LDETFGLIDT AEKSAQILVK 250 260 270 VYSMGGMKQT ISREELIALG QRFGVTPLAS ALAL

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000247 Genomic DNA. Translation: ABG72068.1.
RefSeq	YP_671969.1.
3D structure databases
SMR	Q0TAG1. Positions 1-274.
ModBase	Search...
Genome annotation databases
GeneID	4189732.
GenomeReviews	Gene locus ECP_4112 in contig CP000247_GR.
KEGG	ecp:ECP_4112.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0TAG1.
OMA	Q0TAG1. MSHIARL.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_4112-MON.
Family and domain databases
HAMAP	MF_00770. [Tree]
InterPro	IPR001303. Aldolase_II/adducin_N. IPR013447. RhaD. [Graphical view]
Gene3D	G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
TIGRFAMs	TIGR02624. rhamnu_1P_ald. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RHAD_ECOL5

Accession

Primary (citable) accession number: Q0TAG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 20 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)