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Database: UniProt
Entry: A0A1U9JJQ7_9NEIS
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Original site: A0A1U9JJQ7_9NEIS 
ID   A0A1U9JJQ7_9NEIS        Unreviewed;       558 AA.
AC   A0A1U9JJQ7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BXU06_03995 {ECO:0000313|EMBL:AQR64310.1};
OS   Aquaspirillum sp. LM1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Aquaspirillum.
OX   NCBI_TaxID=1938604 {ECO:0000313|EMBL:AQR64310.1, ECO:0000313|Proteomes:UP000188659};
RN   [1] {ECO:0000313|EMBL:AQR64310.1, ECO:0000313|Proteomes:UP000188659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM1 {ECO:0000313|EMBL:AQR64310.1,
RC   ECO:0000313|Proteomes:UP000188659};
RA   Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
RL   Submitted (JAN-2017) 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; CP019509; AQR64310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9JJQ7; -.
DR   STRING; 1938604.BXU06_03995; -.
DR   KEGG; aql:BXU06_03995; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000188659; Chromosome.
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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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:UP000188659}.
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        513
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   558 AA;  62235 MW;  2FF9BA0644D2FC7C CRC64;
     MTQPRHYDLN HTSIWAKLHQ HQRATRHMHM RELFAADPER FARFSLSLGP LLMDYSKHRI
     TERTLELLFE LANAARLGDW RQRMRAGERI NVSEQRAVLH MALRGQAEDE FDVAGQPVMG
     LVLAVRARMA AFARQVRSGD WRGFDGQPIR TVVNLGIGGS DLGPMLVCQA LRPFAGPLDV
     RFVSNLDGQH LAQTLEGLDP ATTLFIVASK SFTTPETLMN AEAARAWLLQ VASQADVARH
     FVAISSQTER VRAFGIDPAN MFEFWDWVGG RYSVWSAIGL SVMLAIGPEA FEDFLAGARQ
     MDAHFLEAPF AQNIPVILAL LGVWYNTFYR AHTHAIMPYD QGLGRLPAYL QQLDMESNGK
     RVGRYGETLD FDTGPVIWGE VGVNSQHAFF QLLHQGTRLV PCDFIVPMRS HYPIDHHHQA
     LVANCFAQTE ALMRGKTEAE VLAELAGLDG DSIDLLLPQK LFPGNQPSTT LALDAITPHT
     LGMLLAMYEH KVFVQGVIWG INSFDQWGVE YGKQLARQIQ PELADPAQPL AHDASTNALI
     AHYRQRATAA STLPEPQP
//
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