G6PI_ALCBS
ID G6PI_ALCBS Reviewed; 548 AA.
AC Q0VR14;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=ABO_0936;
OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS SK2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=393595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX PubMed=16878126; DOI=10.1038/nbt1232;
RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA Weidner S., Kaiser O., Golyshin P.N.;
RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT Alcanivorax borkumensis.";
RL Nat. Biotechnol. 24:997-1004(2006).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; AM286690; CAL16384.1; -; Genomic_DNA.
DR RefSeq; WP_011588220.1; NC_008260.1.
DR AlphaFoldDB; Q0VR14; -.
DR SMR; Q0VR14; -.
DR STRING; 393595.ABO_0936; -.
DR PRIDE; Q0VR14; -.
DR EnsemblBacteria; CAL16384; CAL16384; ABO_0936.
DR KEGG; abo:ABO_0936; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; VERCKAM; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008871; 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 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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..548
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000252606"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 387
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 511
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 548 AA; 60524 MW; C0BAD4A364DC5A10 CRC64;
MVPEQNDLTE SSVWLQLENL AREEGSLHLS DFFVQELGRC AHFCLESDGL LVDLSKQRVS
SHARDLLVSL ADERGLDRWS EALFAGAEVN CTENRSAKHW LLRDPSDQAA EIHGQLEIMD
SIVSRVLEGQ WRGVLGDAIT DVVNVGVGGS ELGPLMAAFA LHSTPLAEGE VRPSLHFASS
MDGSQISQVL QELNPRTTLV LVSSKSFTTV DTLHNANTAR SWMARALGLE MDNEAMLRCH
FIGISAQPDK MTAWGIPSTN QLQFWDWVGG RYSLWSAIGL PIALTVGMHG FRELLAGAHD
MDLHFRQRPW HENIPVMLAL VDVWNINFLD IRARAVLPYD GRLKYLPAYL EQLEMESNGK
SVSRNGDPVD YHTCPVIWGE VGPNAQHAFF QLLHQGTQPV ACEFLMTARR YTESAHSGAA
VELEGQHALS NANCLAQSRL LAFGEQALDS TLALPAYKRY RGNQPSTTLV LDELSPRTLG
SLLAMYEHKV FAQAVIWGIN PFDQWGVEMG KVIATDMLAV LADPDGAHEV DDSSLSLARH
IACKQATQ