ID A0A177MZG7_9GAMM Unreviewed; 546 AA.
AC A0A177MZG7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:OAI10995.1};
GN ORFNames=A1359_15390 {ECO:0000313|EMBL:OAI10995.1};
OS Methylomonas lenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=980561 {ECO:0000313|EMBL:OAI10995.1, ECO:0000313|Proteomes:UP000078476};
RN [1] {ECO:0000313|EMBL:OAI10995.1, ECO:0000313|Proteomes:UP000078476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-45370 {ECO:0000313|EMBL:OAI10995.1,
RC ECO:0000313|Proteomes:UP000078476};
RA Ploux O.;
RL Submitted (MAR-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}.
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:OAI10995.1}.
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DR EMBL; LUUI01000146; OAI10995.1; -; Genomic_DNA.
DR RefSeq; WP_066986367.1; NZ_LUUI01000146.1.
DR AlphaFoldDB; A0A177MZG7; -.
DR STRING; 980561.A1359_15390; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000078476; 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; 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:UP000078476}.
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 385
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 510
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 546 AA; 61479 MW; A4BB1EAA85AD4719 CRC64;
MSKLINSAEW NAVKQHHLDI AGKFCMKEAF ANDPLRFEKF STTFNDLLFD YSKNLITEQT
MPLLIKLANR AELRKKTEAM FSGSIINTTE KRAVLHTALR NRSNEPVFFR DKDVMPEINK
VLAKMRVFTE QVRSGDWTGY TGKPITDIVN IGIGGSDLGP KMVDTALTPY GQEGMKAHFV
SNVDQTDIVE TLNPLNPETT LFLISSKTFT TQETMTNAHS ARDWFLNAAK DPALISKHFI
AISTNVEKVK EFGIDPNNMF EFWDWVGGRY SLWSVIGMSI ALYIGQDNFE ELLMGAHLAD
EHFRHAPFEQ NIPVIMGLLG VWYNNFFEAE TYAILPYAQS LKYFADYFQQ GDMESNGKSA
TINGEKVDYN TGPIIWGQPG TNGQHAFFQL IHQGTKLVPS DFLAAAQSQY DLPDHHDILI
SNFLAQAEAL MKGKTEAEVR QDLSHEPNLD DALIASKIFD GNKPSNSFLF KKLTPRTLGS
LIAFYEHKIF VQGVIWNINS FDQMGVELGK VLAKAILPEL KNDEVTTSHD SSTNGLINTY
KKLRKA
//
