Q0TL93 (GMHA_ECOL5) 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:	ECP_0252

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate By similarity. HAMAP-Rule MF_00067
Catalytic activity	D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. HAMAP-Rule MF_00067
Cofactor	Binds 1 zinc ion per subunit By similarity.
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-Rule MF_00067
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
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-Rule 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	Complete proteome
Gene Ontology (GO)
Biological_process	D-glycero-D-manno-heptose 7-phosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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: HAMAP carbohydrate binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 192	192	Phosphoheptose isomerase HAMAP-Rule MF_00067		PRO_1000009063
Regions
	Domain	37 – 192	156	SIS
	Region	52 – 54	3	Substrate binding By similarity
	Region	93 – 94	2	Substrate binding By similarity
	Region	119 – 121	3	Substrate binding By similarity
Sites
	Metal binding	61	1	Zinc By similarity
	Metal binding	65	1	Zinc By similarity
	Metal binding	172	1	Zinc By similarity
	Metal binding	180	1	Zinc By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0TL93 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 7A2C05E1079108B4	FASTA	192	20,815
	10 20 30 40 50 60 MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC GNGGSHCDAM 70 80 90 100 110 120 HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI FSRYVEAVGR EGDVLLGIST 130 140 150 160 170 180 SGNSANVIKA IAAAREKGMK VITLTGKDGG KMAGTADIEI RVPHFGYADR IQEIHIKVIH 190 ILIQLIEKEM VK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 536 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000247 Genomic DNA. Translation: ABG68288.1.
RefSeq	YP_668187.1. NC_008253.1.
3D structure databases
ProteinModelPortal	Q0TL93.
SMR	Q0TL93. Positions 1-192.
ModBase	Search...
Protein-protein interaction databases
STRING	362663.ECP_0252.
Proteomic databases
PRIDE	Q0TL93.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG68288; ABG68288; ECP_0252.
GeneID	4190620.
KEGG	ecp:ECP_0252.
PATRIC	18191151. VBIEscCol77757_0253.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0279.
HOGENOM	HOG000237571.
KO	K03271.
OMA	FLAHKEA.
PhylomeDB	Q0TL93.
ProtClustDB	PRK00414.
Enzyme and pathway databases
BioCyc	ECOL362663:GIY5-253-MONOMER.
UniPathway	UPA00041; UER00436.
Family and domain databases
HAMAP	MF_00067. GmhA.
InterPro	IPR004515. Phosphoheptose_Isoase. IPR001347. SIS. [Graphical view]
Pfam	PF13580. SIS_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00441. gmhA. 1 hit.
PROSITE	PS51464. SIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GMHA_ECOL5

Accession

Primary (citable) accession number: Q0TL93

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program