ID A0A0R1RTB4_9LACO Unreviewed; 448 AA.
AC A0A0R1RTB4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=FC69_GL001590 {ECO:0000313|EMBL:KRL59630.1};
OS Latilactobacillus fuchuensis DSM 14340 = JCM 11249.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=1423747 {ECO:0000313|EMBL:KRL59630.1, ECO:0000313|Proteomes:UP000051264};
RN [1] {ECO:0000313|EMBL:KRL59630.1, ECO:0000313|Proteomes:UP000051264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14340 {ECO:0000313|EMBL:KRL59630.1,
RC ECO:0000313|Proteomes:UP000051264};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRL59630.1}.
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; AZEX01000044; KRL59630.1; -; Genomic_DNA.
DR RefSeq; WP_025082913.1; NZ_BAMJ01000008.1.
DR AlphaFoldDB; A0A0R1RTB4; -.
DR STRING; 1423747.FC69_GL001590; -.
DR PATRIC; fig|1423747.3.peg.1618; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000051264; 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}.
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 448 AA; 49355 MW; 3491EE60765F3707 CRC64;
MAHISFDASR LDKFVQSNEL AEMQAMVNAA DSQLRQGTGA GNDFRGFLDL PVNYDKAEFA
RIKKAAAKIK SDSEIFIAIG IGGSYLGAKA AIDFLNTTFF NMIPADQREF PQVIFAGNSI
SSSYLTDLVN LIGDRDFSIN VISKSGTTTE PSIAFRVLKD KLIKKYGKDA AKGRIYATTD
RAKGALKTES DAEGYDEYVV PDDIGGRFSV LTAVGLLPIA VAGGDIDQLM QGAADARAEY
NDTDVTKNDA YKYAALRNIL YRKGYTTELL ENYEPTLQYF SEWWKQLMGE SEGKDQKGIY
PSSANFSTDL HSLGQYIQEG RRNLMETVVN VEKPNSDIDI PTDAQNLDGL GYLEGHTMDF
VNKKAYQGVV LAHTDGGVPV MTVNIPDQTA YTLGYMIYFF EMAVSISGYL NGINPFNQPG
VEAYKKNMFA LLGKPGFEEL GKELNERL
//
