Reviewed, UniProtKB/Swiss-Prot Q9HGZ2 (G6PI_ASPOR)

Names and origin

Protein names

Recommended name:
    Glucose-6-phosphate isomerase
      Short name=GPI
    EC=5.3.1.9
Alternative name(s):
    Phosphoglucose isomerase
      Short name=PGI
    Phosphohexose isomerase
      Short name=PHI

Gene names

Name:	pgiA
ORF Names:	AO090011000659

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	D-glucose 6-phosphate = D-fructose 6-phosphate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the GPI family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glucose-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 – 553	553	Glucose-6-phosphate isomerase		PRO_0000180571
Sites
	Active site	363	1	Proton donor By similarity
	Active site	394	1	By similarity
	Active site	516	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HGZ2-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 06373377B1FF8949	FASTA	553	61,214
	10 20 30 40 50 60 MPAFSQATDL SAWKELQEHH TAVGRNIVLK EAFEKDPQRF EKFSRTFKNT VDNSDILFDF 70 80 90 100 110 120 SKNFLTEETL SLLVKLAKEA NVEELRDAMF KGEHINFTED RAVYHAALRN VSNEPMQVDG 130 140 150 160 170 180 KSVVEDVNSV LEHMKEFSEQ VRSGEWKGYT DKKIDTIINI GIGGSDLGPV MVTEALKPYG 190 200 210 220 230 240 APGMKLHFVS NIDGTHIAEA LKDSNPETTL FLIASKTFTT AETTTNANSA KKWFLETAKD 250 260 270 280 290 300 ESHIAKHFVA LSTNEAEVTK FGIDKKNMFG FESWVGGRYS VWSAIGLSVA LYIGYDNFHQ 310 320 330 340 350 360 FLAGAQAMDK HFREAPLEQN IPAIGGLLSV WYSDFFGAQT HLVAPFDQYL HRFPAYLQQL 370 380 390 400 410 420 SMESNGKAIT RSGEYVKYTT GPILFGEPAT NAQHSFFQLL HQGTKLIPSD FIMAAESHNP 430 440 450 460 470 480 VEGGKHQRML ASNFLAQSEA LMVGKTPEQV KTEGAPDNLV PHKTFLGNRP TTSILAQKIT 490 500 510 520 530 540 PSTLGALIAY YEHLTFTEGA VWNINSFDQW GVELGKVLAK KIQQELETSG AGAGHDASTS 550 GLLAAFKQKA NLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of glycolytic gene from Aspergillus oryzae." Nakajima K., Kunihiro S., Sano M., Eto S., Machida M. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB032269 mRNA. Translation: BAB12229.1. AP007171 Genomic DNA. Translation: BAE65122.1.
RefSeq	XP_001826255.1.
3D structure databases
HSSP	HSSP built from PDB template 1HM5 based on UniProtKB Q9N1E2.
ModBase	Search...
Genome annotation databases
GeneID	5998358.
GenomeReviews	Gene locus pgiA in contig AP007171_GR.
KEGG	aor:AO090011000659.
Enzyme and pathway databases
BRENDA	5.3.1.9. 2240.
Family and domain databases
InterPro	IPR001672. G6P_Isomerase. IPR018189. Phosphoglucose_isomerase_CS. [Graphical view]
PANTHER	PTHR11469. G6P_Isomerase. 1 hit.
Pfam	PF00342. PGI. 1 hit. [Graphical view]
PRINTS	PR00662. G6PISOMERASE.
PROSITE	PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit. PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit. PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G6PI_ASPOR

Accession

Primary (citable) accession number: Q9HGZ2
Secondary accession number(s): Q2TZZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	March 1, 2001
Last modified:	October 13, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)