Reviewed, UniProtKB/Swiss-Prot Q9YE01 (PGMI_AERPE)

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
    Phosphoglucose isomerase
      Short name=PGI
    Mannose-6-phosphate isomerase
    EC=5.3.1.8
    Phosphomannose isomerase
      Short name=PMI

Gene names

Ordered Locus Names:

APE_0768.1

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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=3.5 mM for glucose 6-phosphate KM=0.44 mM for fructose 6-phosphate KM=1.1 mM for mannose 6-phosphate Vmax=225 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius) Vmax=195 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius) Vmax=209 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 80 degrees Celsius) pH dependence: Optimum pH is 7.6. Temperature dependence: Optimum temperature is above 98 degrees Celsius.

Ontologies

Keywords
Molecular function	Isomerase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Molecular function	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 – 333	333	Bifunctional phosphoglucose/phosphomannose isomerase		PRO_0000227544
Regions
	Domain	22 – 160	139	SIS
Sites
	Active site	211	1	Proton acceptor By similarity
	Active site	227	1	Proton donor By similarity
	Active site	322	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YE01-1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 3E94DE8CCF7E5DC3	FASTA	333	35,942
	10 20 30 40 50 60 MEDLYLSWPK WFSEALARYS SLEGALEGVE EIYYCGMGGS GAAGDYIEAL LSIYAPQGPE 70 80 90 100 110 120 FRVVKDFRPP RPPRHRGYGL VLASYSGNTL ETVECGSLLS PAAGRVVAVT SGGRLLEMAK 130 140 150 160 170 180 ERGWLVARLP GGILPRVSFP WMLAASTAML SGALGVDLEA LKRLAGGLDT QGLKGEAERL 190 200 210 220 230 240 AGFISRYRIA SLVTCGPGIP LAVRLKNELA ENAKMPSRLE IYPESSHNDI VALEAAEGLY 250 260 270 280 290 300 GAVFIWIEHE GSLCPAVLDV VEGIYREYGV DTISIESSAR GGPNATVAEY LSRTLVFGLA 310 320 330 SVRLALMRGF NPEETPPIDK YKRRLGEALR SQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.
[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: 14551194] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA79746.2.
PIR	B72668.
RefSeq	NP_147479.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1444882.
GenomeReviews	Gene locus APE_0768.1 in contig BA000002_GR.
KEGG	ape:APE_0768.1.
NMPDR	fig|272557.1.peg.587.
Organism-specific databases
CMR	Search...
Enzyme and pathway databases
BRENDA	5.3.1.8. 256344. 5.3.1.9. 256344.
Family and domain databases
InterPro	IPR011857. Glu6P/Mann6P_isomerase. IPR019490. Glu6P/Mann6P_isomerase_C. [Graphical view]
Pfam	PF10432. bact-PGI_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR02128. G6PI_arch. 1 hit.
PROSITE	PS51464. SIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGMI_AERPE

Accession

Primary (citable) accession number: Q9YE01

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	June 26, 2007
Last modified:	October 13, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)