Q6D1H3 (GMHA_ERWCT) 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:	ECA3473

Organism

Erwinia carotovora subsp. atroseptica (strain SCRI 1043 / ATCC BAA-672) (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

218491 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium › Erwinia carotovora subsp. atroseptica

Protein attributes

Sequence length	193 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 – 193	193	Phosphoheptose isomerase HAMAP-Rule MF_00067		PRO_1000009065
Regions
	Domain	37 – 193	157	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)
	Q6D1H3 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 3F57AF263FB6EDB9	FASTA	193	20,790
	10 20 30 40 50 60 MYQDLIRSEL KEAAETLNNF LSDDANIQSI QNAAVLLANA FKAGGKVISC GNGGSHCDAM 70 80 90 100 110 120 HFAEELTGRY RENRPGYPAI AISDPSHLSC VSNDFGYDFV FSRYVESLGR EGDVLLGIST 130 140 150 160 170 180 SGNSGNIIKA IAAAKAKGMK VITLTGKDGG KMAGSADVEI RVPHFGYADR IQEIHIKAIH 190 ILIQLIEKEM ADQ

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950851 Genomic DNA. Translation: CAG76372.1.
RefSeq	YP_051563.1. NC_004547.2.
3D structure databases
HSSP	HSSP built from PDB template 1X94 based on UniProtKB Q9KPY2.
ProteinModelPortal	Q6D1H3.
SMR	Q6D1H3. Positions 1-190.
ModBase	Search...
Protein-protein interaction databases
STRING	218491.ECA3473.
Proteomic databases
PRIDE	Q6D1H3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG76372; CAG76372; ECA3473.
GeneID	2882938.
KEGG	eca:ECA3473.
PATRIC	20482311. VBIPecAtr54885_3515.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0279.
HOGENOM	HOG000237571.
KO	K03271.
OMA	FLAHKEA.
ProtClustDB	PRK00414.
Enzyme and pathway databases
BioCyc	PATR218491:GJNB-3542-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_ERWCT

Accession

Primary (citable) accession number: Q6D1H3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program