ID A0A1Y1RUX6_9SPIO Unreviewed; 532 AA.
AC A0A1Y1RUX6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:ORC31125.1};
GN ORFNames=B4O97_17560 {ECO:0000313|EMBL:ORC31125.1};
OS Marispirochaeta aestuarii.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Marispirochaeta.
OX NCBI_TaxID=1963862 {ECO:0000313|EMBL:ORC31125.1, ECO:0000313|Proteomes:UP000192343};
RN [1] {ECO:0000313|EMBL:ORC31125.1, ECO:0000313|Proteomes:UP000192343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC444 {ECO:0000313|EMBL:ORC31125.1,
RC ECO:0000313|Proteomes:UP000192343};
RA Shivani Y., Subhash Y., Sasikala C., Ramana C.;
RT "Draft Genome sequence of Marispirochaeta sp. strain JC444.";
RL Submitted (MAR-2017) 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:ORC31125.1}.
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DR EMBL; MWQY01000027; ORC31125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RUX6; -.
DR STRING; 1963862.B4O97_17560; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000192343; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000192343}.
FT ACT_SITE 360
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 391
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 506
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 532 AA; 58139 MW; D9D23F15EDC57B27 CRC64;
MKYLNLDRTD AYGKLKEEYS SGKERLSLPD LLSAERIRSC SIAAGGGLTY NYAAKEVNEK
VLRLLSDLAA ETECIEKYRA LAGGERMNTG EDRRVLHHLT RGELAGPVTE KDRDLGAFYR
EQQKRIADFS RRLRAGEITG STGKSFSTVV QIGIGGSDLG PRALYLALKN WCRTELKSPL
LEARFISNVD PDDAEEVLSS LDFERTLFIL VSKSGTTQET LTNRALVAGM MRSAGIPGLD
PERHFVAVTS ETSPLAGAPG FLDSFFIDDY IGGRYSSTSA VGGVVLSLAF GPEIFERLLA
GAHQADKAAM EGDVRRNAAL MDALIGVWER NICGYPVSAI LPYSQGLHRF PAHLQQLDME
SNGKQVNREG SAVAYSTGPV IFGEPGTNGQ HSFYQLLHQG TDIVPLQFIG FVKSQTGYDT
EYENSTSQQK LKANLTAQIV AFAAGKKNSN LNKNFPGGRP SSLIYGEQLN PEALGALLAH
FENKVMFQGF IWNINSFDQE GVQLGKILTS QVLGAAEKRG DLLDTYARLL KL
//
