ID A0A171AP80_9BACT Unreviewed; 447 AA.
AC A0A171AP80;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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 ORFNames=PJIAN_4605 {ECO:0000313|EMBL:GAT64061.1};
OS Paludibacter jiangxiensis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=681398 {ECO:0000313|EMBL:GAT64061.1, ECO:0000313|Proteomes:UP000076586};
RN [1] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis strain NM7.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis NM7(T), a propionate-
RT producing fermentative bacterium.";
RL Genome Announc. 0:0-0(2017).
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:GAT64061.1}.
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; BDCR01000004; GAT64061.1; -; Genomic_DNA.
DR RefSeq; WP_068705816.1; NZ_BDCR01000004.1.
DR AlphaFoldDB; A0A171AP80; -.
DR STRING; 681398.PJIAN_4605; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000076586; 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 Reference proteome {ECO:0000313|Proteomes:UP000076586}.
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 424
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 447 AA; 48563 MW; EC1E542BBDB19854 CRC64;
MGNISINIDK TFGFISKEAV SGYEAAVKAS NAALHAGTGK GNDFLGWLNL PSSTTAEHLA
DIEATAKILI DNCEVVVVVG IGGSYLGAKA VIDALSNSFD WLQTERKYPV IVYAGQNIGE
DYLFELQSFL KTKKFGIISI SKSGTTTEPA LAFRLLKSQL EAQQGKEAAK KLIVAITDKA
RGALRTLATQ EGYKTFIIED NIGGRYSFLT PVGLLPIATA GFDIKQLVAG AADMEKIAGM
DTPFAENPAA IYAATRNELY KNGKKIEILV NFHPKLHFVA EWWKQLYGES EGKENKGIFP
AAVDFTTDLH SMGQWIQEGE RTIFETVISV KEPNHSVSVP SDDANLDGLN FLVGKSVDQV
NKMAELGTML AHVDGGVPNI KIELPKLDEY NLGQLLYFFE KACGISGYVL GVNPFDQPGV
EAYKKNMFAL LDKPGYEAES KAIKAKL
//
