Phosphoheptose isomerase 1 - Campylobacter jejuni

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Q9PNE6 (GMHA1_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoheptose isomerase 1
EC=5.3.1.28

Alternative name(s):
Sedoheptulose 7-phosphate isomerase 1

Gene names

Name:	gmhA1
Synonyms:	gmhA
Ordered Locus Names:	Cj1149c

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	186 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 By similarity. HAMAP MF_00067
Catalytic activity	D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. HAMAP MF_00067
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00067
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 Bacterial outer membrane biogenesis; LOS core biosynthesis. HAMAP MF_00067
Subunit structure	Homotetramer By similarity. HAMAP MF_00067
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 By similarity. HAMAP MF_00067
Sequence similarities	Belongs to the SIS family. GmhA subfamily. Contains 1 SIS domain.

Ontologies

Keywords
Biological process	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	lipopolysaccharide core region biosynthetic process Inferred from electronic annotation. Source: InterPro
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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliH	Q0PBI9	1	EBI-1193890,EBI-1191439
fliY	Q0PC74	1	EBI-1193890,EBI-1191111

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 186

186

Phosphoheptose isomerase 1 HAMAP MF_00067

PRO_0000136522

Regions

Domain

33 – 186

154

SIS

Region

48 – 50

Substrate binding By similarity

Region

90 – 91

Substrate binding By similarity

Region

116 – 118

Substrate binding By similarity

Sites

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

168

Zinc By similarity

Metal binding

176

Zinc By similarity

Binding site

Substrate By similarity

Binding site

121

Substrate By similarity

Binding site

168

Substrate By similarity

Experimental info

Sequence conflict

V → A in AAR82882. Ref.2

Sequence conflict

A → E in AAR99164. Ref.1

Sequence conflict

A → E in AAR82882. Ref.2

Sequence conflict

E → D in AAR99164. Ref.1

Sequence conflict

109

K → N in AAR99164. Ref.1

Sequence conflict

109

K → N in AAR82882. Ref.2

Sequence conflict

128

L → F in AAR99164. Ref.1

Sequence conflict

128

L → F in AAR82882. Ref.2

Secondary structure

186

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9PNE6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D7759471EC88924D
Show »

FASTA

186

20,085

        10         20         30         40         50         60 
MINLVEKEWQ EHQKIVQASE ILKGQIAKVG ELLCECLKKG GKILICGNGG SAADAQHFAA 

        70         80         90        100        110        120 
ELSGRYKKER KALAGIALTT DTSALSAIGN DYGFEFVFSR QVEALGNEKD VLIGISTSGK 

       130        140        150        160        170        180 
SPNVLEALKK AKELNMLCLG LSGKGGGMMN KLCDHNLVVP SDDTARIQEM HILIIHTLCQ 


IIDESF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Gilbert M. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43446 / MK104 / Serotype O:19.
[2]	"Evidence for acquisition of the lipooligosaccharide biosynthesis locus in Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-Barre syndrome, by horizontal exchange." Gilbert M., Godschalk P.C., Karwaski M.-F., Ang C.W., Van Belkum A., Li J., Wakarchuk W.W., Endtz H.P. Infect. Immun. 72:1162-1165(2004) [PubMed: 14742567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GB11.
[3]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.
[4]	"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.
[5]	"Deciphering Campylobacter jejuni cell surface interactions from the genome sequence." Linton D., Karlyshev A.V., Wren B.W. Curr. Opin. Microbiol. 4:35-40(2001) [PubMed: 11173031] [Abstract] Cited for: CELL SURFACE.
[6]	"Crystal structures of two putative phosphoheptose isomerases." Seetharaman J., Rajashankar K.R., Solorzano V., Kniewel R., Lima C.D., Bonanno J.B., Burley S.K., Swaminathan S. Proteins 63:1092-1096(2006) [PubMed: 16477602] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-186.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF167344 Genomic DNA. Translation: AAR99164.1.
AY422197 Genomic DNA. Translation: AAR82882.1.
AL111168 Genomic DNA. Translation: CAL35264.1.

PIR

G81319.

RefSeq

YP_002344540.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TK9	X-ray	2.10	A/B/C/D	2-186	[»]

ProteinModelPortal

Q9PNE6.

SMR

Q9PNE6. Positions 1-186.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9PNE6. 105 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

905439.

GenomeReviews

Gene locus Cj1149c in contig AL111168_GR.

KEGG

cje:Cj1149c.

PATRIC

20059254. VBICamJej33762_1130.

Phylogenomic databases

HOGENOM

HBG671955.

OMA

HITIIHI.

ProtClustDB

PRK13937.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ1149C-MONOMER.

Family and domain databases

HAMAP

MF_00067. GmhA.
[Tree]

InterPro

IPR004515. Phosphoheptose_Isoase_subgr.
IPR020620. Phosphoheptose_isomerase.
IPR001347. SIS.
[Graphical view]

K03271.

Pfam

PF01380. SIS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00441. GmhA. 1 hit.

PROSITE

PS51464. SIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GMHA1_CAMJE

Accession

Primary (citable) accession number: Q9PNE6
Secondary accession number(s): Q0P9A7, Q6TG10, Q7BPS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents