Reviewed, UniProtKB/Swiss-Prot P45314 (KDOP_HAEIN)

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

Ordered Locus Names:

HI1679

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the hydrolysis of KDO 8-P to KDO and inorganic phosphate. Ref.2
Catalytic activity	3-deoxy-D-manno-octulosonate 8-phosphate + H2O = 3-deoxy-D-manno-octulosonate + phosphate.
Cofactor	Magnesium Probable.
Miscellaneous	Cobalt was used in the crystallography experiment but magnesium is likely to be the physiological metal.
Sequence similarities	Belongs to the kdsC family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro
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 – 180

180

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase

PRO_0000201703

Sites

Metal binding

14

1

Magnesium Probable

Metal binding

16

1

Magnesium Probable

Metal binding

107

1

Magnesium Probable

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

180

Helix Strand Turn

Details...

Helix

2 – 6

5

Beta strand

10 – 13

4

Turn

16 – 18

3

Beta strand

22 – 27

6

Beta strand

30 – 37

8

Helix

38 – 49

12

Beta strand

53 – 57

5

Helix

63 – 72

10

Beta strand

76 – 78

3

Helix

84 – 95

12

Helix

99 – 101

3

Beta strand

102 – 106

5

Helix

109 – 111

3

Helix

112 – 117

6

Beta strand

118 – 123

6

Helix

129 – 132

4

Beta strand

135 – 138

4

Turn

143 – 146

4

Helix

147 – 158

12

Helix

163 – 166

4

Helix

168 – 173

6

Helix

175 – 177

3

Sequences

	Sequence		Length	Mass (Da)
	P45314-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 23CD435E4E83A095	FASTA	180	19,432
	10 20 30 40 50 60 MQQKLENIKF VITDVDGVLT DGQLHYDANG EAIKSFHVRD GLGIKMLMDA DIQVAVLSGR 70 80 90 100 110 120 DSPILRRRIA DLGIKLFFLG KLEKETACFD LMKQAGVTAE QTAYIGDDSV DLPAFAACGT 130 140 150 160 170 180 SFAVADAPIY VKNAVDHVLS THGGKGAFRE MSDMILQAQG KSSVFDTAQG FLKSVKSMGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase." Wu J., Woodard R.W. J. Biol. Chem. 278:18117-18123(2003) [PubMed: 12639950] [Abstract] Cited for: FUNCTION, COFACTOR.
[3]	"From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase." Parsons J.F., Lim K., Tempczyk A., Krajewski W., Eisenstein E., Herzberg O. Proteins 46:393-404(2002) [PubMed: 11835514] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS), METAL-BINDING.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L42023 Genomic DNA. Translation: AAC23325.1.

PIR

G64174.

RefSeq

NP_439821.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J8D	X-ray	2.30	A/B/C/D	1-180	[»]
1K1E	X-ray	1.67	A/B/C/D/E/F/G/H/I/J/K/L	1-180	[»]

ModBase

Search...

Genome annotation databases

GeneID

950506.

GenomeReviews

Gene locus HI1679 in contig L42023_GR.

KEGG

hin:HI1679.

NMPDR

fig|71421.1.peg.1592.

TIGR

HI1679.

Phylogenomic databases

HOGENOM

P45314.

OMA

P45314. KTFNTLD.

Enzyme and pathway databases

BioCyc

HINF71421:HI_1679-MON.

BRENDA

3.1.3.45. 109.

Family and domain databases

InterPro

IPR005834. Dehalogen-like_hydro.
IPR006549. HAD-SF_hydro_IIIA.
IPR010023. Phosphatase_KdsC.
[Graphical view]

Pfam

PF00702. Hydrolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01670. YrbI-phosphatas. 1 hit.

ProtoNet

Search...

Entry information

Entry name

KDOP_HAEIN

Accession

Primary (citable) accession number: P45314

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 72 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)