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Database: UniProt
Entry: I1XLT0_METNJ
LinkDB: I1XLT0_METNJ
Original site: I1XLT0_METNJ 
ID   I1XLT0_METNJ            Unreviewed;       545 AA.
AC   I1XLT0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   OrderedLocusNames=Q7A_2556 {ECO:0000313|EMBL:AFI85349.1};
GN   ORFNames=CDW43_11280 {ECO:0000313|EMBL:AUZ85115.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI85349.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI85349.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI85349.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT   sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(2012).
RN   [2] {ECO:0000313|EMBL:AFI85349.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI85349.1};
RX   PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri
RT   sp. nov., isolated from the biofilm of the methanol-fed denitrification
RT   system treating the seawater at the Montreal Biodome.";
RL   Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN   [3] {ECO:0000313|EMBL:AFI85349.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI85349.1};
RA   Villeneuve C., Villemur R.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUZ85115.1, ECO:0000313|Proteomes:UP000238402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP59 {ECO:0000313|EMBL:AUZ85115.1,
RC   ECO:0000313|Proteomes:UP000238402};
RA   Villemur R.;
RT   "The sequence of the genome of Methylophaga nitratireducenticrescens GP59
RT   and its two plasmids.";
RL   Submitted (JUN-2017) 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; CP003390; AFI85349.1; -; Genomic_DNA.
DR   EMBL; CP021973; AUZ85115.1; -; Genomic_DNA.
DR   RefSeq; WP_014707711.1; NZ_CP021973.1.
DR   AlphaFoldDB; I1XLT0; -.
DR   STRING; 754476.Q7A_2556; -.
DR   KEGG; mej:Q7A_2556; -.
DR   PATRIC; fig|754476.3.peg.2510; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_6; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000009144; Chromosome.
DR   Proteomes; UP000238402; 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; 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        351
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        510
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   545 AA;  60999 MW;  75D548E8DF56D2D4 CRC64;
     MTPLNIAEWQ SLDRHYSDIK YLSMREQFAL DSGRFERFSI RSGDLLLDYS KNRITQETID
     KLIALADAVN IQEWIERMFS GDQINHTEGR AVLHTALRNR SNTPVMVDGQ DVMPQVNAVL
     DKMAAFCEQV HSGKWLGFSN KKITDIVNIG IGGSDLGPAM ICDALEPYGI DGIQAHFVSN
     VDGTDLSTTL EKLNPETTLF VVASKTFTTQ ETITNAQSAR NWFLKAGTQA DVAKHFVAVS
     TNAKEVAKFG IDTANMFEIW DWVGGRYSLW SAIGLPIALY VGMDNFLRLL DGGHEMDKHF
     RTKPLAENIP LIMGMLGIWY INFFNAQTHA IVPYDHSLAR FPSHMQQLDM ESNGKFINRQ
     GARISYKTGP VIWGTPGTNG QHAYFQLIHQ GTQLIPVDFV LPVNSHYPEC DHQSILLANG
     LAQSEALMKG KTAEEVREEL VKEGYEGKAL DALLPHKVFP GNRPSNVLLF PKLTPEMLGQ
     LVALYEHKVF VQGVIWNINS FDQWGVELGK QLAKAILPDL QSNAEISVHD SSTTELIRLI
     RTLRQ
//
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