Reviewed, UniProtKB/Swiss-Prot P0ABZ5 (KDSC_ECO57)

Names and origin

Protein names

Recommended name:
    3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
    EC=3.1.3.45
Alternative name(s):
    KDO 8-P phosphatase

Gene names

Name:	kdsC
Ordered Locus Names:	Z4561, ECs4077

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the hydrolysis of KDO 8-P to KDO and inorganic phosphate By similarity.
Catalytic activity	3-deoxy-D-manno-octulosonate 8-phosphate + H2O = 3-deoxy-D-manno-octulosonate + phosphate.
Cofactor	Magnesium Probable.
Pathway	Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the kdsC family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-deoxy-manno-octulosonate-8-phosphatase activity Inferred from electronic annotation. Source: EC magnesium 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 – 188	188	3-deoxy-D-manno-octulosonate 8-phosphate phosphatase		PRO_0000201697

Sequences

	Sequence		Length	Mass (Da)
	P0ABZ5-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 75AF512CF4E5E6E2	FASTA	188	19,997
	10 20 30 40 50 60 MSKAGASLAT CYGPVSADVI AKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY 70 80 90 100 110 120 GIRCALTSDI EVAIITGRKA KLVEDRCATL GITHLYQGQS NKLIAFSDLL EKLAIAPENV 130 140 150 160 170 180 AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTRIA GGRGAVREVC DLLLLAQGKL DEAKGQSI

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG58332.1. BA000007 Genomic DNA. Translation: BAB37500.1.
PIR	E91138. H85983.
RefSeq	NP_289772.1. NP_312104.1.
3D structure databases
HSSP	HSSP built from PDB template 1K1E based on UniProtKB P45314.
ModBase	Search...
Genome annotation databases
GeneID	916077. 958043.
GenomeReviews	Gene locus Z4561 in contig AE005174_GR. Gene locus ECs4077 in contig BA000007_GR.
KEGG	ece:Z4561. ecs:ECs4077.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0ABZ5.
OMA	P0ABZ5. KTFNTLD.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4077-MON.
Family and domain databases
InterPro	IPR013200. HAD-SF_hydro-like_3. IPR006549. HAD-SF_hydro_IIIA. IPR010023. Phosphatase_KdsC. [Graphical view]
Pfam	PF08282. Hydrolase_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR01662. HAD-SF-IIIA. 1 hit. TIGR01670. YrbI-phosphatas. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KDSC_ECO57

Accession

Primary (citable) accession number: P0ABZ5
Secondary accession number(s): P45396, P45398

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	June 16, 2009
This is version 26 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)