UniProt: A0A0X3ANE8

Database: UniProt
Entry: A0A0X3ANE8_9FLAO

LinkDB:  A0A0X3ANE8_9FLAO 
Original site:  A0A0X3ANE8_9FLAO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (3)   
All databases (18)   

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ID   A0A0X3ANE8_9FLAO        Unreviewed;       549 AA.
AC   A0A0X3ANE8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=Ga0061079_102228 {ECO:0000313|EMBL:CVK15677.1};
OS   Apibacter mensalis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Apibacter.
OX   NCBI_TaxID=1586267 {ECO:0000313|EMBL:CVK15677.1, ECO:0000313|Proteomes:UP000182761};
RN   [1] {ECO:0000313|EMBL:CVK15677.1, ECO:0000313|Proteomes:UP000182761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-53146 {ECO:0000313|EMBL:CVK15677.1,
RC   ECO:0000313|Proteomes:UP000182761};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; FCOR01000002; CVK15677.1; -; Genomic_DNA.
DR   RefSeq; WP_055424899.1; NZ_LIVM01000002.1.
DR   AlphaFoldDB; A0A0X3ANE8; -.
DR   STRING; 1586267.GCA_001418685_00508; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000182761; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182761}.
FT   ACT_SITE        356
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        515
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   549 AA;  62744 MW;  7747227927619A49 CRC64;
     MALSKINPTE TQAWHLLKEH YDQIKDKHLR QWFNEDPQRF EKFSIQFNDL LFDYSKNRID
     EKALKLLIQL AEETHVKEAI EKQFSGDKIN ETENRAVLHT ALRNRKNTPV LINGEDVMPK
     VNRVLSQMQK FSESVISGEW KGYTGKAITD VVNIGIGGSD LGPLMVVEGL KYYKTRLNLH
     FVSNIDGTHI VETLKPLNPE TTMFIVASKT FTTQETMTNA QTAKDWFLKS AKLESEVAKH
     FVALSTNQEA VTQFGINKDN MFEFWDWVGG RYSIWSAIGL SICLAVGYDN FTELLEGGNE
     VDLHFRNTKF DQNIPVILAL LGIWYNNFFG AEDVALLPYE QYLHRFAAYF QQGDMESNGK
     YIDRNGDKID YQTGPIIFGE PGTNGQHAFY QLIHQGTKLI PCDFFAGART LNQVSDHHEK
     LISNFFAQTE ALAFGKTEDT VIKELKEQGK SDEEINKLKP YKIFEGNRPT NSFLYKILTP
     KLLGKLIAIY EQKIFVQGVI WNIFSFDQWG VELGKQLANK VLPELSGDQK ITTHDSSTNG
     LINAYKKMR
//

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