ID A0A1X7GJ90_9PROT Unreviewed; 384 AA.
AC A0A1X7GJ90;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=SAMN02744631_0018 {ECO:0000313|EMBL:SMF70566.1};
OS Candidatus Pelagibacter sp. HIMB1321.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1388755 {ECO:0000313|EMBL:SMF70566.1, ECO:0000313|Proteomes:UP000192921};
RN [1] {ECO:0000313|Proteomes:UP000192921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB1321 {ECO:0000313|Proteomes:UP000192921};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
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DR EMBL; LT840186; SMF70566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7GJ90; -.
DR STRING; 1388755.SAMN02744631_0018; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000192921; Chromosome i.
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; cd05016; SIS_PGI_2; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
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; 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 384 AA; 44778 MW; 0892F8C00704D501 CRC64;
MINSRINFKN FRFKKRNLQI KKYLIEITKS SNAIINSLKK DYKYSYKKLL LRKLTKYQNL
RVIGMGGSVL GFKAIHSFLF SKVKKKFTFH DNIESFDKID FKKKYLNIII SKSGNTTETI
ANSNLFINKK NENIFVTENK VNYLNKLAAK LKSDIIHHNN FIGGRYSVLS EVGMLPAELA
GLKVENFKQF NNLIKNKKFI SSLVNNVSSI LHLVKKKKFN SIILNYDKNS EDLFFWYQQL
VAESLGKKSK GILPIISNMP KDNHSLMQLY LDGFTNNFFT FFSVKEKNIN RLNNSLILNE
KKFLKNKSIQ EIKLSQRKAT ERVFNKKLLP FRSFEIKKRD ERTIGELFTF FILETILLGK
SLGVNPYDQP SVELIKKETK KILA
//
