GLF_ZYMMO
ID GLF_ZYMMO Reviewed; 473 AA.
AC P21906; Q5NQL4;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Glucose facilitated diffusion protein {ECO:0000303|PubMed:2254282};
GN Name=glf {ECO:0000303|PubMed:2254282}; OrderedLocusNames=ZMO0366;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=2254282; DOI=10.1128/jb.172.12.7227-7240.1990;
RA Barnell W.O., Yi K.C., Conway T.;
RT "Sequence and genetic organization of a Zymomonas mobilis gene cluster that
RT encodes several enzymes of glucose metabolism.";
RL J. Bacteriol. 172:7227-7240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=8144485; DOI=10.1128/jb.176.7.2133-2135.1994;
RA Snoep J.L., Arfman N., Yomano L.P., Fliege R.K., Conway T., Ingram L.O.;
RT "Reconstruction of glucose uptake and phosphorylation in a glucose-negative
RT mutant of Escherichia coli by using Zymomonas mobilis genes encoding the
RT glucose facilitator protein and glucokinase.";
RL J. Bacteriol. 176:2133-2135(1994).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=7768841; DOI=10.1128/jb.177.11.3351-3354.1995;
RA Weisser P., Kraemer R., Sahm H., Sprenger G.A.;
RT "Functional expression of the glucose transporter of Zymomonas mobilis
RT leads to restoration of glucose and fructose uptake in Escherichia coli
RT mutants and provides evidence for its facilitator action.";
RL J. Bacteriol. 177:3351-3354(1995).
CC -!- FUNCTION: Allows uptake of glucose by the cell; allows growth on
CC glucose minimal medium by E.coli cells impaired in glucose transport
CC (PubMed:8144485). Also transports fructose, but has a strong preference
CC for glucose (PubMed:7768841). {ECO:0000269|PubMed:7768841,
CC ECO:0000269|PubMed:8144485}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 mM for glucose uptake in E.coli at 10 degrees Celsius
CC {ECO:0000269|PubMed:7768841};
CC KM=39 mM for fructose uptake in E.coli at 15 degrees Celsius
CC {ECO:0000269|PubMed:7768841};
CC Vmax=42 nmol/min/mg enzyme for glucose uptake in E.coli at 10 degrees
CC Celsius {ECO:0000269|PubMed:7768841};
CC Vmax=93 nmol/min/mg enzyme for fructose uptake in E.coli at 15
CC degrees Celsius {ECO:0000269|PubMed:7768841};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; M60615; AAA27691.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29864.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88990.1; -; Genomic_DNA.
DR PIR; A37855; A37855.
DR RefSeq; WP_011240287.1; NZ_CP035711.1.
DR AlphaFoldDB; P21906; -.
DR SMR; P21906; -.
DR STRING; 264203.ZMO0366; -.
DR TCDB; 2.A.1.1.4; the major facilitator superfamily (mfs).
DR EnsemblBacteria; AAV88990; AAV88990; ZMO0366.
DR GeneID; 58026215; -.
DR KEGG; zmo:ZMO0366; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_30_5_5; -.
DR OMA; SCHEQEM; -.
DR OrthoDB; 955823at2; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="Glucose facilitated diffusion protein"
FT /id="PRO_0000050302"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..112
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..187
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..303
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..366
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..429
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 145
FT /note="A -> R (in Ref. 1; AAA27691 and 2; AAG29864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 50115 MW; 3886E6A18ACD6926 CRC64;
MSSESSQGLV TRLALIAAIG GLLFGYDSAV IAAIGTPVDI HFIAPRHLSA TAAASLSGMV
VVAVLVGCVT GSLLSGWIGI RFGRRGGLLM SSICFVAAGF GAALTEKLFG TGGSALQIFC
FFRFLAGLGI GVVSTLTPTY IAEIAPPDKR GQMVSGQQMA IVTGALTGYI FTWLLAHFGS
IDWVNASGWC WSPASEGLIG IAFLLLLLTA PDTPHWLVMK GRHSEASKIL ARLEPQADPN
LTIQKIKAGF DKAMDKSSAG LFAFGITVVF AGVSVAAFQQ LVGINAVLYY APQMFQNLGF
GADTALLQTI SIGVVNFIFT MIASRVVDRF GRKPLLIWGA LGMAAMMAVL GCCFWFKVGG
VLPLASVLLY IAVFGMSWGP VCWVVLSEMF PSSIKGAAMP IAVTGQWLAN ILVNFLFKVA
DGSPALNQTF NHGFSYLVFA ALSILGGLIV ARFVPETKGR SLDEIEEMWR SQK
