G6PI_BRUA4
ID G6PI_BRUA4 Reviewed; 549 AA.
AC A6WVU6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Oant_0369;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS13100.1; -; Genomic_DNA.
DR RefSeq; WP_012090690.1; NC_009667.1.
DR AlphaFoldDB; A6WVU6; -.
DR SMR; A6WVU6; -.
DR STRING; 439375.Oant_0369; -.
DR EnsemblBacteria; ABS13100; ABS13100; Oant_0369.
DR KEGG; oan:Oant_0369; -.
DR PATRIC; fig|439375.7.peg.392; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
DR PhylomeDB; A6WVU6; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002301; Chromosome 1.
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..549
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000013993"
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 384
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 513
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 549 AA; 59734 MW; AAE345733D237F17 CRC64;
MARDATKLEA TVAKLKKHWA DSAPHDMRAA FKSDPGRFER YSLSLDDLLF DWSKCRVNDE
TIGLLKELAI AADVEGRRAA MFAGEHINNT EDRAVLHVAL RDTSSKEVLV DGHNVLPDVK
EVLDRMAAFA DGIRSGAIKG ATGKKITDIV NIGIGGSDLG PVMATLALSP YHDGPRAHFV
SNIDGAHIAD TLGILDPATT LVIIASKTFT TIETMTNAQT ARKWVADALG EAAVGAHFAA
VSTALDRVAA FGIAEDRVFG FWDWVGGRYS VWSAIGLPVM IAIGPEDFRK FLAGAHSMDV
HFRDAPLEKN LAVWLGLIGY WHRAICGYGS RAIIPYDQRL ARLPAYLQQL DMESNGKSVT
VDGKPVSGPT GPVVWGEPGT NGQHAFFQLL HQGTDTIPLE FIVAAKGHEK HLDHQHEMLL
ANCLAQSEAL MKGRTLDEAR AQLKAKNLPE SEVERIAPHR VFSGNRPSLT LVHDKLDPFA
LGRLVALYEH RVFVEAQIFG INAFDQWGVE LGKELATELL PVVSGEESSD GRDASTQGLV
AHLHARRKA
