ID A0A0K0Y5B6_9RHOB Unreviewed; 531 AA.
AC A0A0K0Y5B6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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 ECO:0000313|EMBL:AKS46159.1};
GN ORFNames=OSB_16100 {ECO:0000313|EMBL:AKS46159.1}, SAMN05444287_1267
GN {ECO:0000313|EMBL:SIO08676.1};
OS Octadecabacter temperatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS46159.1, ECO:0000313|Proteomes:UP000067444};
RN [1] {ECO:0000313|EMBL:AKS46159.1, ECO:0000313|Proteomes:UP000067444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB1 {ECO:0000313|EMBL:AKS46159.1,
RC ECO:0000313|Proteomes:UP000067444};
RX PubMed=26358607;
RA Voget S., Billerbeck S., Simon M., Daniel R.;
RT "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT Mesophilic Species of the Genus Octadecabacter.";
RL Genome Announc. 3:e01051-15(2015).
RN [2] {ECO:0000313|EMBL:SIO08676.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO08676.1};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000184809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; CP012160; AKS46159.1; -; Genomic_DNA.
DR EMBL; FSRP01000001; SIO08676.1; -; Genomic_DNA.
DR RefSeq; WP_049834476.1; NZ_FSRP01000001.1.
DR AlphaFoldDB; A0A0K0Y5B6; -.
DR STRING; 1458307.OSB_16100; -.
DR KEGG; otm:OSB_16100; -.
DR PATRIC; fig|1458307.3.peg.1624; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000067444; Chromosome.
DR Proteomes; UP000184809; 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 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:UP000067444}.
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 369
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 497
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 531 AA; 57696 MW; C6D3ADF833B36001 CRC64;
MWGKLHIHHE AVENRRFETL FDVKRADDFT ASVGDMRLDY AKTNIDERGR ALLIDLLDQV
DLAGKRDAMF DGTAINETEG RAVLHTALRN LDGGPVMVDG ADVMPEVLGT LDRMEKFAAD
VRSGAFKGQG GKITDVVNIG IGGSDLGPAM GVLALAPYHD GPRCHFVSNV DPADISQVLR
SCDPTTTLVI VASKTFTTIE TMTNARTAKA WMGESVSDPA AQFAALSTSE DGTAAFGIDA
ARVFGFEDWV GGRYSMWGPI GLSMMIAIGP DAFRAFLRGA RDMDRHFQAA DWSENMPVML
ALVGIWHNQI CGYSTRAVLP YDNNLSRLPA YLQQLEMESN GKGVSMDGED LSINSGPVVW
GEPGTNGQHA FYQLIHQGTR VIPCEFLVAA RGHDDDLHHQ HQLLVANCLA QSEALMKGRD
LDEARGKVAD KFEGAELERQ AKHRVFAGNR PSVTIAYPKL DPFTLGQIIA LYEHRVFVEG
VVLGINSYDQ WGVELGKELA TALQPIVEGA DASGKDESTA ALVGFLQQHG V
//
