ID A0A0P0FZ71_9BACT Unreviewed; 539 AA.
AC A0A0P0FZ71;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:ALJ56652.1};
GN ORFNames=AMD24_00480 {ECO:0000313|EMBL:ALJ56652.1};
OS Candidatus Xiphinematobacter sp. Idaho Grape.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Xiphinematobacter.
OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56652.1, ECO:0000313|Proteomes:UP000062177};
RN [1] {ECO:0000313|EMBL:ALJ56652.1, ECO:0000313|Proteomes:UP000062177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56652.1,
RC ECO:0000313|Proteomes:UP000062177};
RX PubMed=26362082; DOI=10.1093/gbe/evv176;
RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT Role in Nutritional Symbiosis.";
RL Genome Biol. Evol. 7:2727-2746(2015).
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|HAMAP-Rule:MF_00473,
CC 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|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|HAMAP-
CC Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
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DR EMBL; CP012665; ALJ56652.1; -; Genomic_DNA.
DR RefSeq; WP_062100501.1; NZ_CP012665.1.
DR AlphaFoldDB; A0A0P0FZ71; -.
DR STRING; 1704307.AMD24_00480; -.
DR KEGG; xii:AMD24_00480; -.
DR PATRIC; fig|1704307.3.peg.530; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000062177; 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 HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
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; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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:UP000062177}.
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 352
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 456
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 539 AA; 59484 MW; 91077C6F1EB26AF1 CRC64;
MSAMSLWTRF QEYFLRYEDS GFSLDISRMG FSEDFLPSMQ SRAKQALLSM EELERGNIAN
QDENRMVGHY WLRDPGLAPT AELRMGIANA LDTVLKFSAD VHLGTVRGVT GKKFTDVLSI
GIGGSALGPQ LVSDALGNAQ DPLSVHFLDN TDPDGFARVL AKLSGKLDAT LVVVISKSGN
TKEPHNGLLT VQHAFKQAGI SPFNKHFVAV TEVDSTLDSI ARAEGWLRRF PIHSWVGGRT
SVMSAGGLVP MSLQGLDVAS FLRGARTMDM RTRHSDLRKN AALLLALMWY YAREKRGKGD
MVILPYKDRL LLLSRYLQQL IMESLGKERD LDGGLVHQGI SVYGNKGSTD QHTYVQQLLD
GVDNFFVTFI EVRQVASFQE LEVEPGITSG DYLQGFLRGT RSALCEKGRD SLTISINQLN
ASSLGALIAL YERAVGFYGS LTHINAYHQP GVEAGKRAAF HVLELQKKIL TFLQTHSGLP
MNAEKIAQNI GGDAEETFHI LQHLAANRSA NISHSLGQQP SEDHFSWKCP STLEKRTQE
//
