ID Y0KHA1_9PROT Unreviewed; 550 AA.
AC Y0KHA1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=Meth11DRAFT_1331 {ECO:0000313|EMBL:EUJ10509.1};
OS Methylophilaceae bacterium 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae.
OX NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ10509.1, ECO:0000313|Proteomes:UP000022668};
RN [1] {ECO:0000313|EMBL:EUJ10509.1, ECO:0000313|Proteomes:UP000022668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11 {ECO:0000313|EMBL:EUJ10509.1,
RC ECO:0000313|Proteomes:UP000022668};
RG DOE Joint Genome Institute;
RA Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., Schaumberg A.,
RA Pati A., Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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: 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:EUJ10509.1}.
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DR EMBL; JCKJ01000001; EUJ10509.1; -; Genomic_DNA.
DR AlphaFoldDB; Y0KHA1; -.
DR STRING; 1101195.Meth11DRAFT_1331; -.
DR PATRIC; fig|1101195.3.peg.1298; -.
DR eggNOG; COG0166; Bacteria.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000022668; 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:UP000022668}.
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 384
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 550 AA; 61677 MW; B24E3EFF8C95B8FE CRC64;
MATLTQHPSW QALCQHQKLT STQHMRDLFN ADPKRYETFS MQCGDLLLDY SKHRITTETL
NLLFQMAREA NIEGWRDRMF SGEKINITEN RAVLHTALRN RSNAPVYVDG KDVMPDVNAV
LAQMRIFTEK VRNGSWTGYT GKAITDIVNI GIGGSDLGPV MVCDALKPYA SPNLNVHFVS
NIDGAHLMRA LEKCNPETTL FIVASKTFTT QETMTNATSA RTWFLNAAKD NAHVAKHFVA
LSTNAKAVEA FGIDTANMFA FWDWVGGRYS LWSAIGLSIA LYVGMDHFEE LLAGGHAMDN
HFKTAPLEQN MPVIMAMIGV WYNNFFHVDT HAILPYDQGL ARFAAYLQQA DMESNGKFVC
RDGTDVQYKT GPVIWGEAGT NGQHAFYQLI HQGTQIVTAD FLMPIHSHYQ VGTNGDQHHK
ILLANFLAQT QALMLGKTRE EARAELEQQG LSGEALEQLL PHKVFPGNRP TTSIMFDKLT
PHTLGKLIAL YEHKIFVQGI IWDINSYDQW GVEYGKQIAQ QILPLLTNDD VIDRFDGSTN
GLINYAKQRT
//
