gmhA

Functionⁱ

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.

2 Publications

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.

Catalytic activityⁱ

2
D-sedoheptulose 7-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
D-glycero-α-D-manno-heptose 7-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
D-glycero-β-D-manno-heptose 7-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants."
  Taylor P.L., Blakely K.M., de Leon G.P., Walker J.R., McArthur F., Evdokimova E., Zhang K., Valvano M.A., Wright G.D., Junop M.S.
  J. Biol. Chem. 283:2835-2845(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SEDOHEPTULOSE-7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF HIS-61; GLU-65; ARG-69; ASP-94; THR-120; ASP-169; GLN-172 AND HIS-180.
EC:
5.3.1.28
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants."
  Taylor P.L., Blakely K.M., de Leon G.P., Walker J.R., McArthur F., Evdokimova E., Zhang K., Valvano M.A., Wright G.D., Junop M.S.
  J. Biol. Chem. 283:2835-2845(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SEDOHEPTULOSE-7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF HIS-61; GLU-65; ARG-69; ASP-94; THR-120; ASP-169; GLN-172 AND HIS-180.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
2
D-sedoheptulose 7-phosphate
zoom
=
D-glycero-α-D-manno-heptose 7-phosphate
zoom
+
D-glycero-β-D-manno-heptose 7-phosphate
zoom

Cofactorⁱ

Zn²⁺By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayⁱ: D-glycero-D-manno-heptose 7-phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate. This subpathway is part of the pathway D-glycero-D-manno-heptose 7-phosphate biosynthesis, which is itself part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate, the pathway D-glycero-D-manno-heptose 7-phosphate biosynthesis and in Carbohydrate biosynthesis.

Pathwayⁱ: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	61	ZincBy similarity	1
Binding siteⁱ	61	Substrate	1
Metal bindingⁱ	65	ZincBy similarity	1
Binding siteⁱ	65	SubstrateBy similarity	1
Binding siteⁱ	120	Substrate	1
Binding siteⁱ	124	SubstrateBy similarity	1
Binding siteⁱ	169	Substrate	1
Metal bindingⁱ	172	ZincBy similarity	1
Binding siteⁱ	172	Substrate	1
Metal bindingⁱ	180	ZincBy similarity	1
Binding siteⁱ	180	Substrate	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase
Biological process	Carbohydrate metabolism, Lipopolysaccharide biosynthesis
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G6106-MONOMER
BRENDAⁱ	5.3.1.28, 2026
UniPathwayⁱ	UPA00041;UER00436 UPA00958

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Phosphoheptose isomerase (EC:5.3.1.28) Alternative name(s): Sedoheptulose 7-phosphate isomerase
Gene namesⁱ	Name:gmhA Synonyms:lpcA, tfrA, yafI Ordered Locus Names:b0222, JW0212
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	61	H → Q: Almost no effect. 1 Publication	1
Mutagenesisⁱ	65	E → N or Q: No activity. 1 Publication	1
Mutagenesisⁱ	69	R → Q: Almost no effect. 1 Publication	1
Mutagenesisⁱ	94	D → N: No activity. 1 Publication	1
Mutagenesisⁱ	120	T → A: No activity. 1 Publication	1
Mutagenesisⁱ	169	D → N: No activity. 1 Publication	1
Mutagenesisⁱ	172	Q → E: No activity. 1 Publication	1
Mutagenesisⁱ	180	H → Q: No activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000136526	1 – 192	Phosphoheptose isomeraseAdd BLAST		192

Proteomic databases

jPOSTⁱ	P63224
PaxDbⁱ	P63224
PRIDEⁱ	P63224

Interactionⁱ

Subunit structureⁱ

Homotetramer.

1 Publication

Protein-protein interaction databases

BioGRIDⁱ	4263370, 277 interactors
Database of interacting proteins More...DIPⁱ	DIP-48179N
STRINGⁱ	511145.b0222

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 22	Combined sources	20
Helixⁱ	24 – 42	Combined sources	19
Beta strandⁱ	47 – 52	Combined sources	6
Helixⁱ	54 – 70	Combined sources	17
Beta strandⁱ	74 – 76	Combined sources	3
Beta strandⁱ	78 – 81	Combined sources	4
Helixⁱ	88 – 91	Combined sources	4
Helixⁱ	100 – 108	Combined sources	9
Beta strandⁱ	114 – 118	Combined sources	5
Beta strandⁱ	120 – 122	Combined sources	3
Helixⁱ	125 – 137	Combined sources	13
Beta strandⁱ	140 – 146	Combined sources	7
Helixⁱ	150 – 152	Combined sources	3
Beta strandⁱ	156 – 162	Combined sources	7
Helixⁱ	168 – 191	Combined sources	24

Show more details

3D structure databases

AlphaFoldDBⁱ	P63224
SMRⁱ	P63224
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P63224

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	37 – 192	SISAdd BLAST		156

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	54 – 55	Substrate binding	2
Regionⁱ	93 – 94	Substrate bindingBy similarity	2
Regionⁱ	119 – 121	Substrate bindingBy similarity	3

Sequence similaritiesⁱ

Belongs to the SIS family. GmhA subfamily.Curated

Phylogenomic databases

eggNOGⁱ	COG0279, Bacteria
HOGENOMⁱ	CLU_080999_4_0_6
InParanoidⁱ	P63224
OMAⁱ	FLAHKEA
PhylomeDBⁱ	P63224

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd05006, SIS_GmhA, 1 hit
HAMAPⁱ	MF_00067, GmhA, 1 hit
InterProⁱ	View protein in InterPro IPR035461, GmhA/DiaA IPR004515, Phosphoheptose_Isoase IPR001347, SIS_dom IPR046348, SIS_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13580, SIS_2, 1 hit
SUPFAMⁱ	SSF53697, SSF53697, 1 hit
TIGRFAMsⁱ	TIGR00441, gmhA, 1 hit
PROSITEⁱ	View protein in PROSITE PS51464, SIS, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P63224-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC 
        60         70         80         90        100
GNGGSHCDAM HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI 
       110        120        130        140        150
FSRYVEAVGR EGDVLLGIST SGNSANVIKA IAAAREKGMK VITLTGKDGG 
       160        170        180        190 
KMAGTADIEI RVPHFGYADR IQEIHIKVIH ILIQLIEKEM VK

Length:192

Mass (Da):20,815

Last modified:September 27, 2004 - v1

Checksum:ⁱ7A2C05E1079108B4

GO

Sequence cautionⁱ

The sequence AAB08644 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U32590 Genomic DNA Translation: AAC43630.1 D38582 Genomic DNA Translation: BAA07584.1 U70214 Genomic DNA Translation: AAB08644.1 Different initiation. U00096 Genomic DNA Translation: AAC73326.1 AP009048 Genomic DNA Translation: BAA77892.1
PIRⁱ	G64746
NCBI Reference Sequences More...RefSeqⁱ	NP_414757.1, NC_000913.3 WP_000284050.1, NZ_STEB01000020.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73326; AAC73326; b0222 BAA77892; BAA77892; BAA77892
GeneIDⁱ	66671459 949134
KEGGⁱ	ecj:JW0212 eco:b0222
PATRICⁱ	fig\|1411691.4.peg.2061

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P63224	Phosphoheptose isomerase		ECO24		192	UniRef100_A7ZHY1
Phosphoheptose isomerase		ECO45		192
Phosphoheptose isomerase		ECO55		192
Phosphoheptose isomerase		ECO57		192
Phosphoheptose isomerase		ECO5E		192
+179

Protein	Similar proteins		Species	Score	Length	Source
P63224	Phosphoheptose isomerase		ECO24		192	UniRef90_A7ZHY1
Phosphoheptose isomerase		ECO45		192
Phosphoheptose isomerase		ECO55		192
Phosphoheptose isomerase		ECO57		192
Phosphoheptose isomerase		ECO5E		192
+222

Protein	Similar proteins		Species	Score	Length	Source
P63224	Phosphoheptose isomerase		YERPE		193	UniRef50_Q8ZBY7
Phosphoheptose isomerase		PHOLL		193
Phosphoheptose isomerase		EDWI9		193
Phosphoheptose isomerase		KLEP7		193
Phosphoheptose isomerase		KLEP3		193
+1368

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U32590 Genomic DNA Translation: AAC43630.1 D38582 Genomic DNA Translation: BAA07584.1 U70214 Genomic DNA Translation: AAB08644.1 Different initiation. U00096 Genomic DNA Translation: AAC73326.1 AP009048 Genomic DNA Translation: BAA77892.1
PIRⁱ	G64746
RefSeqⁱ	NP_414757.1, NC_000913.3 WP_000284050.1, NZ_STEB01000020.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2I22	X-ray	2.80	A/B/C/D	1-192	[»]
	2I2W	X-ray	1.95	A/B/C/D	1-192	[»]
AlphaFoldDBⁱ	P63224
SMRⁱ	P63224
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4263370, 277 interactors
DIPⁱ	DIP-48179N
STRINGⁱ	511145.b0222

Proteomic databases

jPOSTⁱ	P63224
PaxDbⁱ	P63224
PRIDEⁱ	P63224

Genome annotation databases

EnsemblBacteriaⁱ	AAC73326; AAC73326; b0222 BAA77892; BAA77892; BAA77892
GeneIDⁱ	66671459 949134
KEGGⁱ	ecj:JW0212 eco:b0222
PATRICⁱ	fig\|1411691.4.peg.2061

Organism-specific databases

EchoBASEⁱ	EB2940

EchoBASEⁱ

EB2940

Phylogenomic databases

eggNOGⁱ	COG0279, Bacteria
HOGENOMⁱ	CLU_080999_4_0_6
InParanoidⁱ	P63224
OMAⁱ	FLAHKEA
PhylomeDBⁱ	P63224

Enzyme and pathway databases

UniPathwayⁱ	UPA00041;UER00436 UPA00958
BioCycⁱ	EcoCyc:G6106-MONOMER
BRENDAⁱ	5.3.1.28, 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P63224
Protein Ontology More...PROⁱ	PR:P63224

Family and domain databases

CDDⁱ	cd05006, SIS_GmhA, 1 hit
HAMAPⁱ	MF_00067, GmhA, 1 hit
InterProⁱ	View protein in InterPro IPR035461, GmhA/DiaA IPR004515, Phosphoheptose_Isoase IPR001347, SIS_dom IPR046348, SIS_dom_sf
Pfamⁱ	View protein in Pfam PF13580, SIS_2, 1 hit
SUPFAMⁱ	SSF53697, SSF53697, 1 hit
TIGRFAMsⁱ	TIGR00441, gmhA, 1 hit
PROSITEⁱ	View protein in PROSITE PS51464, SIS, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GMHA_ECOLI
Accessionⁱ	P63224Primary (citable) accession number: P63224 Secondary accession number(s): P51001
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
	Last sequence update:	September 27, 2004
	Last modified:	May 25, 2022
	This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P63224 (GMHA_ECOLI)

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Phosphoheptose isomerase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: D-glycero-D-manno-heptose 7-phosphate biosynthesis

Pathwayi: LPS core biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Cytosol

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: D-glycero-D-manno-heptose 7-phosphate biosynthesis

Pathwayⁱ: LPS core biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ