ID A0A0P7YPN8_9GAMM Unreviewed; 555 AA.
AC A0A0P7YPN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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-2 {ECO:0000313|EMBL:KPQ23721.1};
GN Synonyms=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN ORFNames=HLUCCA13_12290 {ECO:0000313|EMBL:KPQ23721.1};
OS Halomonas sp. HL-48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1479235 {ECO:0000313|EMBL:KPQ23721.1, ECO:0000313|Proteomes:UP000050569};
RN [1] {ECO:0000313|EMBL:KPQ23721.1, ECO:0000313|Proteomes:UP000050569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-48 {ECO:0000313|EMBL:KPQ23721.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ23721.1}.
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DR EMBL; LJZS01000015; KPQ23721.1; -; Genomic_DNA.
DR RefSeq; WP_027336085.1; NZ_LJZS01000015.1.
DR AlphaFoldDB; A0A0P7YPN8; -.
DR STRING; 1479235.GCA_000686925_01083; -.
DR PATRIC; fig|1479235.4.peg.313; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000050569; 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}.
FT REGION 529..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 555 AA; 62223 MW; 0E6A8C53AEB5F026 CRC64;
MFQLTRSVTW QALERLRDKT ANDRIRDYFT HDPQRFDKMS LRVGGLFLDY SKHHVSDDVL
AKLIELADHS ALVQRRAQMF SGDIINVTED RPVLHTALRN LSDEPVYVDG EDVMPEITRT
REQIKLFSEA VRSGEWKGYS GQRIKDVVNI GIGGSDLGPN MAVRALLKYR HPDLHFHFVS
NVDGTHIQKV LSRLDPATTL FIVSTKTFST QETLLNAKTA RRWFLENAGE DADVGAHFIA
ASTNRRAAME FGIREENVFE FWAWVGGRYS MWSSIGLPIA LSIGFEGFIE LLEGAHEMDR
HFIEAPFSEN MPVLMALIGI WYINFIGAET QAVVPYDQAL HQLPSFLQQL DMESNGKSVD
IFGHPVNYKT GPIVWGQTGS NGQHAFFQLL HQGTRYVPID FIASLKPEPG VEDHHFALLT
NMLAQANAFM EGSQGDAKEL SQHDPYSCPG NRPSSTLLLD ELTPKNLGAL IALYEHKVFV
QGVIWNINSF DQWGVQLGKR IAGEISERID TNAADFDAST QGLLELLRGH FPGNGGSAES
GDKAQTDKKP SRKKR
//
