ID A0A0R3QPJ2_9BILA Unreviewed; 748 AA.
AC A0A0R3QPJ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018388, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000962701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0000962701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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|RuleBase:RU000612};
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|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
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DR AlphaFoldDB; A0A0R3QPJ2; -.
DR STRING; 42155.A0A0R3QPJ2; -.
DR WBParaSite; BTMF_0000962701-mRNA-1; BTMF_0000962701-mRNA-1; BTMF_0000962701.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000050602; Unplaced.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05015; SIS_PGI_1; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR006761; Tsg.
DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR Pfam; PF04668; Tsg; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
SQ SEQUENCE 748 AA; 84451 MW; 5E96B2487FA9B358 CRC64;
LKYLQHRCQL NYSSGLLLFS LIDKNEMVAN IIGWVPLLVL CTLLQDLLQA ALDCNETECG
PRVSKCMLLK ACNCSINRDS ILHNNCSCCN ECIQCLDKQY MQCCACVGLC NPHKEAVHLN
SYVDRFDQDD EDIIVFDKVA LVNKVGTTYT FPALREYSFD RRGQNMKALR RTHQETNCTV
VYLDKCMSHE QCSRQCLILG ASMLRWFHTG CCECIGHTCL PYGSTTARCK YCTDFDNSLI
LILRQYIYVR QDYSDCKFVP KLNLGFSDQL TDIVLSHQGG NGCIYLGDKT TNRTTNCSYT
SASSFKEDTT DDYAVIFSIA NNQGNSCESK LYSSSIVLLH ITSVSGSPTQ RIDFRVECTH
AYFAWVLGMG AGANRHIANE MSLHKDSAFI QLQQHFESEC KFLKMVDLFK QDPQRFQKYS
LKMDTPDGPI LFDYSKNIIN EETMKRLFNL ANSRNVLNMR QDMFSGKKIN FTEGRAVLHT
ALRNVNNKPL TLDGQNVTDD VNNVLEHMRT FCDQVIRGTW KGYTGEAITD VVNIGIGGSD
LGPLMVTEAL KHYQVGPNVH FVSNIDGTHL AEVLKKIKPE TTIFIIASKT FTTQETITNA
TSAKEWFLSK AVNPAAVAKH FVALSTNGPK VREFGIDENN MFGFWDWVGG RYSLWSAIGL
SIAVHIGFDN FSQLLKGASA ADEHFLNEPI EKNIPIIMAL LGVLYINCFK AETHALLPYD
QYLHRFAAYF QQGDMESNGK FMMRFPII
//