Q9HIC2 (PGMI_THEAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional phosphoglucose/phosphomannose isomerase

Alternative name(s):
Glucose-6-phosphate isomerase
Short name=GPI
EC=5.3.1.9
Mannose-6-phosphate isomerase
EC=5.3.1.8
Phosphoglucose isomerase
Short name=PGI
Phosphomannose isomerase
Short name=PMI

Gene names

Ordered Locus Names:

Ta1419

Organism

Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]

Taxonomic identifier

273075 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › Thermoplasma acidophilum

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.
Catalytic activity	D-glucose 6-phosphate = D-fructose 6-phosphate. D-mannose 6-phosphate = D-fructose 6-phosphate.
Enzyme regulation	Inhibited by erythrose 4-phosphate and 6-phosphogluconate.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the PGI/PMI family. Contains 1 SIS domain.
Biophysicochemical properties	Kinetic parameters: KM=0.72 mM for glucose 6-phosphate Ref.2 KM=0.2 mM for fructose 6-phosphate KM=0.25 mM for mannose 6-phosphate Vmax=83 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius) Vmax=57 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius) Vmax=75 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 50 degrees Celsius) pH dependence: Optimum pH is 7.6. Temperature dependence: Optimum temperature is 75 degrees Celsius.

Ontologies

Keywords
Molecular function	Isomerase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro glucose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC mannose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 310	310	Bifunctional phosphoglucose/phosphomannose isomerase		PRO_0000227545
Regions
	Domain	22 – 152	131	SIS
Sites
	Active site	202	1	Proton acceptor By similarity
	Active site	218	1	Proton donor By similarity
	Active site	306	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HIC2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: A88423F901339B1F	FASTA	310	35,045
	10 20 30 40 50 60 MLRSHCMEFS EELKTLKDQV RFDGSFRTGT FSNIVIAGMG GSGIAGRIFS EMYSAKPVFV 70 80 90 100 110 120 CDDYHIPEFV DGNTEFIAVS YSGNTEETLS AAEEAIKKGA KVHAITSGGR LSEMGVDTIK 130 140 150 160 170 180 IPGGLQPRSA VGYLTMPIIN TFIRPKHEDI EEAAGLLSDL DKNNTVQENI ATEIYAGRRI 190 200 210 220 230 240 PVIYGSTPYR SVAYRWKTQF NENAKILAYS NYFSELNHND TMPLRDTYRK DEFYFMAFDS 250 260 270 280 290 300 TDERIRKRIE VTQKITGTSF KKIEARGSSL IARIFYLIHF GDYVTYHLAR IRNVDPQDVS 310 AIEDLKKRIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum." Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W. Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[2]	"Bifunctional phosphoglucose/phosphomannose isomerases from the archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily." Hansen T., Wendor ff D., Schoenheit P. J. Biol. Chem. 279:2262-2272(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL445067 Genomic DNA. Translation: CAC12539.1.
RefSeq	NP_394873.1. NC_002578.1.
3D structure databases
ProteinModelPortal	Q9HIC2.
ModBase	Search...
Protein-protein interaction databases
STRING	273075.Ta1419.
Proteomic databases
PRIDE	Q9HIC2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC12539; CAC12539; CAC12539.
GeneID	1456878.
KEGG	tac:Ta1419.
Phylogenomic databases
eggNOG	COG0166.
HOGENOM	HOG000020037.
KO	K15916.
OMA	PELNHNE.
ProtClustDB	PRK08674.
Enzyme and pathway databases
BRENDA	5.3.1.8. 6324.
SABIO-RK	Q9HIC2.
Family and domain databases
InterPro	IPR011857. Glu6P/Mann6P_isomerase. IPR019490. Glu6P/Mann6P_isomerase_C. IPR001347. SIS. [Graphical view]
Pfam	PF10432. bact-PGI_C. 1 hit. PF01380. SIS. 1 hit. [Graphical view]
TIGRFAMs	TIGR02128. G6PI_arch. 1 hit.
PROSITE	PS51464. SIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGMI_THEAC

Accession

Primary (citable) accession number: Q9HIC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program