ID Q5B093_EMENI Unreviewed; 553 AA.
AC Q5B093; C8V308;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018388, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN ORFNames=ANIA_06037 {ECO:0000313|EMBL:CBF70313.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF70313.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00024178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000256|ARBA:ARBA00029321,
CC ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
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DR EMBL; BN001301; CBF70313.1; -; Genomic_DNA.
DR RefSeq; XP_663641.1; XM_658549.1.
DR AlphaFoldDB; Q5B093; -.
DR STRING; 227321.Q5B093; -.
DR EnsemblFungi; CBF70313; CBF70313; ANIA_06037.
DR GeneID; 2871189; -.
DR KEGG; ani:AN6037.2; -.
DR VEuPathDB; FungiDB:AN6037; -.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; Q5B093; -.
DR OMA; DWYRQLW; -.
DR OrthoDB; 1657888at2759; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0051211; P:anisotropic cell growth; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:AspGD.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560}.
SQ SEQUENCE 553 AA; 61259 MW; 641E438620ACC2D3 CRC64;
MPSFSQAVEL PAWKELQDHH GSVGRNIVLK ECFEKDPQRF EKFSRTFQNT VDNNEILFDF
SKNFLTEETL ALLVKLAKQA GVEELRDQMF AGEPINFTEN RAVYHAALRN VSNQPMQVNG
KSVVEDVNSV LEHMKEFSEQ VRSGEWKGYT GKKINTIINI GIGGSDLGPV MVTEALKPYG
HPDLKLHFVS NIDGTHIAEA LKDSDPETTL FLIASKTFTT AETTTNANTA KSWFLEHAKD
GAHIAKHFVA LSTNAEEVAK FGIDTKNMFG FESWVGGRYS VWSAIGLSVA LYIGYDNFHQ
FLAGAHAMDK HFRETPLEQN IPVLGGLLSV WYSDFFGAQT HLVAPFDQYL HRFPAYLQQL
SMESNGKAIT RTGEYVKYTT GPVLFGEPAT NAQHSFFQLL HQGTKLIPAD FIMAAESHNP
VEGGKHQRML ASNFLAQSEA LMVGKTPEQV KAEGAADNLV PHKTFLGNRP TTSILAQKIT
PAALGALITY YEHLTFTEGA IWNINSFDQW GVELGKVLAK KIQKELETEG EGSGHDSSTS
GLLLAFKKKA KLA
//
