G6PI_BARHE
ID G6PI_BARHE Reviewed; 559 AA.
AC Q8L1Z9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=BH01370;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Houston 1;
RX PubMed=11983902; DOI=10.1073/pnas.082112499;
RA Canback B., Andersson S.G.E., Kurland C.G.;
RT "The global phylogeny of glycolytic enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6097-6102(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Houston 1;
RA Alsmark C.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; AY074771; AAL74284.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF26951.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8L1Z9; -.
DR SMR; Q8L1Z9; -.
DR STRING; 283166.BH01370; -.
DR PaxDb; Q8L1Z9; -.
DR PRIDE; Q8L1Z9; -.
DR EnsemblBacteria; CAF26951; CAF26951; BH01370.
DR KEGG; bhe:BH01370; -.
DR eggNOG; COG0166; Bacteria.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000421; 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: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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..559
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180598"
FT ACT_SITE 363
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 394
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 523
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 559 AA; 62489 MW; 6064CB7C96CAC459 CRC64;
MRYKSMGDSL SIRNEKAFEA ALQALRRHAI KDGVYDIRRH FIEDEQRFSN FSLNLDDFLF
DFSKCGVTFK TLQLLDDLAV AADVLGRRDA MFSGKAINTT EKRSVLHIAL RLPADEVFML
DGTDLVHDIQ GVLADMERFS DMVRDGSYKG NSGEKIIDIV NIGIGGSDLG PAMVTYALKP
YHDGPNCHFV SNADSAHISD TLSVLNPATT LFVIASKTFT TAETIANAQV ARQWIMSHLG
KEAVCKHFIA VSSALDKVAE FGIDSSRTFR FWDWVGGRYS IWSAIGLVVM LAIGGQNFRQ
FLEGAQHMDR HFKTAPLRKN IPIRFALLGF WHRVVCGYAS RAVIPYAQRL ARFPAYLQQL
DMESNGKQVS LDGKTLTFSS GPVVWGDSGT NGQHAFFQLL HQGTDVIPVE FILFIKGHEQ
NLHPMYDMLV ANCLAQSKAL MKGRSVEDAR RMLLKSGIDE RESENLALHK SFAGNRPNMM
LVQDLLTPFA LGRLIALYEH RIFVEGILMN INSFDQWGVE LGKELANELL PILRGENKTN
NRDSSTLGLL AHIQARRGE
