UniProt: A0A1S2LHU8

Database: UniProt
Entry: A0A1S2LHU8_9BACI

LinkDB:  A0A1S2LHU8_9BACI 
Original site:  A0A1S2LHU8_9BACI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (3)   
Literature (2)   
   PubMed (2)   
All databases (21)   

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ID   A0A1S2LHU8_9BACI        Unreviewed;       450 AA.
AC   A0A1S2LHU8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=AWH56_012030 {ECO:0000313|EMBL:QOY38195.1}, AWH56_14940
GN   {ECO:0000313|EMBL:OIJ11971.1};
OS   Anaerobacillus isosaccharinicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX   NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ11971.1, ECO:0000313|Proteomes:UP000180175};
RN   [1] {ECO:0000313|EMBL:OIJ11971.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:OIJ11971.1,
RC   ECO:0000313|Proteomes:UP000180175};
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT   Anaerobacillus genus.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QOY38195.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY38195.1,
RC   ECO:0000313|Proteomes:UP000180175};
RX   PubMed=28104661;
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT   Anaerobacillus Genus.";
RL   Genome Announc. 5:e01493-16(2017).
RN   [3] {ECO:0000313|EMBL:QOY38195.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY38195.1,
RC   ECO:0000313|Proteomes:UP000180175};
RX   PubMed=29580368;
RA   Bassil N.M., Lloyd J.R.;
RT   "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT   degrades isosaccharinic acid.";
RL   Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN   [4] {ECO:0000313|EMBL:QOY38195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY38195.1};
RA   Bassil N.M., Lloyd J.R.;
RL   Submitted (OCT-2020) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}.
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DR   EMBL; LQXD01000131; OIJ11971.1; -; Genomic_DNA.
DR   EMBL; CP063356; QOY38195.1; -; Genomic_DNA.
DR   RefSeq; WP_071317847.1; NZ_CP063356.1.
DR   AlphaFoldDB; A0A1S2LHU8; -.
DR   KEGG; aia:AWH56_012030; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000180175; Chromosome.
DR   Proteomes; UP000180175; 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   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
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   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00473};
KW   Reference proteome {ECO:0000313|Proteomes:UP000180175}.
FT   ACT_SITE        291
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   MOD_RES         39
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   450 AA;  50226 MW;  61BEB627C779E891 CRC64;
     MSEKLHFDYS KALDFIQEHE VTYLQDAVTA AHLALHNKTG AGNEYVGWVD LPENYDREEF
     TRIKKAAEKI KSDSDVLLVV GIGGSYLGAR AAIEALNHTF YNVLSKETRK TPQVIFVGHN
     ISSTYVRDLF DVLEGKDVSV NVISKSGTTT EPAIAFRIFR EYLEKKYGVE EARKRIFATT
     DKERGALKTL AADEGYESFV VPDDVGGRYS VLTAVGLLPI AVSGVDIDAM MQGASDARTD
     LENPDMNTNN AYQYAAVRNA LYNKGKTIEL MVNYEPSLHY VAEWWKQLFG ESEGKDQKGI
     FPASVDFSTD LHSMGQYVQD GRRDLFETVL QVEKVEKEIF IEEASSDLDG LNYLAGKTMD
     FVNKKAFQGT MLAHTDGGVP NLVVSIPELT PYHFGYMVYF FEKACAISGY LLGVNPFDQP
     GVEAYKKNMF ALLGKPGFEE EKAKLEARLK
//

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