Q93UJ2 (GMHA_BURPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoheptose isomerase
EC=5.3.1.28

Alternative name(s):
Sedoheptulose 7-phosphate isomerase

Gene names

Name:	gmhA
Ordered Locus Names:	BPSL2795

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. Ref.4
Catalytic activity	D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. Ref.4
Cofactor	Binds 1 zinc ion per subunit. Ref.4
Pathway	Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. HAMAP MF_00067 Capsule biogenesis; capsule polysaccharide biosynthesis. HAMAP MF_00067
Subunit structure	Homotetramer. Ref.4
Subcellular location	Cytoplasm By similarity HAMAP MF_00067.
Miscellaneous	The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate. HAMAP MF_00067
Sequence similarities	Belongs to the SIS family. GmhA subfamily. Contains 1 SIS domain.

Ontologies

Keywords
Biological process	Capsule biogenesis/degradation Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D-sedoheptulose 7-phosphate isomerase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sugar binding 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 – 197

197

Phosphoheptose isomerase HAMAP MF_00067

PRO_0000136521

Regions

Domain

40 – 197

158

SIS

Region

55 – 57

3

Substrate binding HAMAP MF_00067

Region

97 – 98

2

Substrate binding HAMAP MF_00067

Region

123 – 125

3

Substrate binding HAMAP MF_00067

Sites

Metal binding

64

1

Zinc

Metal binding

68

1

Zinc

Metal binding

175

1

Zinc

Metal binding

183

1

Zinc

Binding site

68

1

Substrate

Binding site

128

1

Substrate

Binding site

175

1

Substrate

Experimental info

Mutagenesis

61

1

D → A: Less than 6% of wild-type activity. Ref.4

Mutagenesis

64

1

H → Q: Less than 10% of wild-type activity. Ref.4

Mutagenesis

68

1

E → Q: No activity. Ref.4

Mutagenesis

98

1

D → N: No activity. Ref.4

Mutagenesis

124

1

T → A: No activity. Ref.4

Mutagenesis

175

1

Q → E: No activity. Ref.4

Sequence conflict

34

1

R → Q in AAK49808. Ref.1

Sequence conflict

115

1

E → K in AAK49808. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

197

Helix Strand Turn

Details...

Helix

4 – 24

21

Helix

27 – 45

19

Beta strand

50 – 52

3

Helix

59 – 65

7

Beta strand

73 – 75

3

Beta strand

82 – 84

3

Helix

89 – 94

6

Turn

102 – 105

4

Helix

106 – 111

6

Beta strand

118 – 120

3

Helix

129 – 140

12

Helix

156 – 159

4

Helix

171 – 175

5

Helix

189 – 193

5

Sequences

	Sequence		Length	Mass (Da)
	Q93UJ2 [UniParc]. Last modified November 23, 2004. Version 2. Checksum: 22A249C834AC585B	FASTA	197	20,813
	10 20 30 40 50 60 MENRELTYIT NSIAEAQRVM AAMLADERLL ATVRKVADAC IASIAQGGKV LLAGNGGSAA 70 80 90 100 110 120 DAQHIAGEFV SRFAFDRPGL PAVALTTDTS ILTAIGNDYG YEKLFSRQVQ ALGNEGDVLI 130 140 150 160 170 180 GYSTSGKSPN ILAAFREAKA KGMTCVGFTG NRGGEMRELC DLLLEVPSAD TPKIQEGHLV 190 LGHIVCGLVE HSIFGKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Detection of bacterial virulence genes by subtractive hybridization: identification of capsular polysaccharide of Burkholderia pseudomallei as a major virulence determinant." Reckseidler S.L., DeShazer D., Sokol P.A., Woods D.E. Infect. Immun. 69:34-44(2001) [PubMed: 11119486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.
[3]	"Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides." Valvano M.A., Messner P., Kosma P. Microbiology 148:1979-1989(2002) [PubMed: 12101286] [Abstract] Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
[4]	"The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site." Harmer N.J. J. Mol. Biol. 400:379-392(2010) [PubMed: 20447408] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC AND D-GLYCERO-ALPHA-D-MANNO-HEPTOSE 7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, REACTION MECHANISM, MUTAGENESIS OF ASP-61; HIS-64; GLU-68; ASP-98; THR-124 AND GLN-175.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF228583 Genomic DNA. Translation: AAK49808.1.
BX571965 Genomic DNA. Translation: CAH36804.1.

RefSeq

YP_109390.1. NC_006350.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2X3Y	X-ray	2.40	A/B/C/D/E/F/G/H	1-197	[»]
2XBL	X-ray	1.62	A/B/C/D	1-197	[»]

ProteinModelPortal

Q93UJ2.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3092932.

GenomeReviews

Gene locus BPSL2795 in contig BX571965_GR.

KEGG

bps:BPSL2795.

NMPDR

fig|272560.3.peg.5476.

PATRIC

19265991. VBIBurPse99623_3191.

Phylogenomic databases

HOGENOM

HBG671955.

OMA

ECHICIG.

ProtClustDB

PRK13937.

Enzyme and pathway databases

BioCyc

BPSE272560:BPSL2795-MONOMER.

Family and domain databases

HAMAP

MF_00067. GmhA.
[Tree]

InterPro

IPR020620. Phosphoheptose_isomerase.
IPR001347. SIS.
[Graphical view]

KO

K03271.

Pfam

PF01380. SIS. 1 hit.
[Graphical view]

PROSITE

PS51464. SIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GMHA_BURPS

Accession

Primary (citable) accession number: Q93UJ2
Secondary accession number(s): Q63R78

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program