GenomeNet

Database: UniProt
Entry: A0A0T9QAH6_9GAMM
LinkDB: A0A0T9QAH6_9GAMM
Original site: A0A0T9QAH6_9GAMM 
ID   A0A0T9QAH6_9GAMM        Unreviewed;       548 AA.
AC   A0A0T9QAH6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN   Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473,
GN   ECO:0000313|EMBL:CNI03133.1};
GN   ORFNames=ERS008529_02857 {ECO:0000313|EMBL:CNI03133.1};
OS   Yersinia pekkanenii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=1288385 {ECO:0000313|EMBL:CNI03133.1, ECO:0000313|Proteomes:UP000045840};
RN   [1] {ECO:0000313|Proteomes:UP000045840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A125KOH2 {ECO:0000313|Proteomes:UP000045840};
RG   Pathogen Informatics;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000256|HAMAP-Rule:MF_00473}.
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|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00473}.
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|HAMAP-Rule:MF_00473,
CC       ECO:0000256|RuleBase:RU000612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CQAZ01000025; CNI03133.1; -; Genomic_DNA.
DR   RefSeq; WP_049613826.1; NZ_CWJL01000025.1.
DR   AlphaFoldDB; A0A0T9QAH6; -.
DR   STRING; 1288385.ERS137968_03858; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000045840; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473}.
FT   ACT_SITE        355
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   548 AA;  61201 MW;  A53FF1CF8E1B0D1E CRC64;
     MKNINPSQTA AWKALQQHFE QMKDVTISSL FAKDDQRFSQ FSATFNDQML VDFSKNRITS
     ETMEKLQALA KETDLAGAIK SMFSGEKINR TEDRAVLHIA LRNRSNTPIV VDGKDVMPEV
     NAVLAKMKQF CDRVIGGDWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF
     VSNVDGTHIA ETLKPLNPET TLFLVASKTF TTQETMTNAH SARDWFLSTA GDEKHVAKHF
     AALSTNAKAV GEFGIDTDNM FEFWDWVGGR YSLWSAIGLS IALSVGFEQF EQLLSGAHAM
     DKHFAETPAE KNLPILLALI GIWYNNFFGA ETEAILPYDQ YMHRFPAYFQ QGNMESNGKY
     VDRNGHPVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKLIP CDFIAPAISH NPLSDHHEKL
     LSNFFAQTEA LAFGKSLAEV EAEFAAAGKT PEQVAYVAPF KVFEGNRPTN SILLREITPF
     SLGALIALYE HKIFTQGAIL NIYTFDQWGV ELGKQLANRI LPELADDKNV TSHDSSTNAL
     INRFKNWR
//
DBGET integrated database retrieval system