GHXQ_ECOLI
ID GHXQ_ECOLI Reviewed; 455 AA.
AC Q46817; Q2M9V6; Q46818; Q6BF61;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Guanine/hypoxanthine permease GhxQ;
GN Name=ghxQ; Synonyms=ygfQ, ygfR; OrderedLocusNames=b4464, JW5467;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND GENE
RP NAME.
RC STRAIN=K12;
RX PubMed=24214977; DOI=10.1074/jbc.m113.523340;
RA Papakostas K., Botou M., Frillingos S.;
RT "Functional identification of the hypoxanthine/guanine transporters YjcD
RT and YgfQ and the adenine transporters PurP and YicO of Escherichia coli K-
RT 12.";
RL J. Biol. Chem. 288:36827-36840(2013).
CC -!- FUNCTION: High-affinity transporter for guanine and hypoxanthine.
CC {ECO:0000269|PubMed:24214977}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for guanine {ECO:0000269|PubMed:24214977};
CC KM=23.2 uM for hypoxanthine {ECO:0000269|PubMed:24214977};
CC Vmax=3.4 nmol/min/mg enzyme with guanine as substrate
CC {ECO:0000269|PubMed:24214977};
CC Vmax=13.8 nmol/min/mg enzyme with hypoxanthine as substrate
CC {ECO:0000269|PubMed:24214977};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24214977};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24214977}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83065.1; Type=Frameshift; Note=Produces two separate ORFs (ygfQ and ygfR).; Evidence={ECO:0000305};
CC Sequence=AAA83066.1; Type=Frameshift; Note=Produces two separate ORFs (ygfQ and ygfR).; Evidence={ECO:0000305};
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DR EMBL; U28375; AAA83065.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U28375; AAA83066.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48153.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76950.1; -; Genomic_DNA.
DR PIR; D65072; D65072.
DR PIR; E65072; E65072.
DR RefSeq; WP_000012163.1; NZ_STEB01000001.1.
DR RefSeq; YP_026186.1; NC_000913.3.
DR AlphaFoldDB; Q46817; -.
DR SMR; Q46817; -.
DR BioGRID; 4259228; 165.
DR STRING; 511145.b4464; -.
DR TCDB; 2.A.40.7.7; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR jPOST; Q46817; -.
DR PaxDb; Q46817; -.
DR PRIDE; Q46817; -.
DR DNASU; 2847748; -.
DR EnsemblBacteria; AAT48153; AAT48153; b4464.
DR EnsemblBacteria; BAE76950; BAE76950; BAE76950.
DR GeneID; 2847748; -.
DR GeneID; 66673243; -.
DR KEGG; ecj:JW5467; -.
DR KEGG; eco:b4464; -.
DR PATRIC; fig|1411691.4.peg.3850; -.
DR EchoBASE; EB2879; -.
DR eggNOG; COG2252; Bacteria.
DR HOGENOM; CLU_024508_0_1_6; -.
DR InParanoid; Q46817; -.
DR OMA; PDAMGMV; -.
DR PhylomeDB; Q46817; -.
DR BioCyc; EcoCyc:G7504-MON; -.
DR BioCyc; MetaCyc:G7504-MON; -.
DR SABIO-RK; Q46817; -.
DR PRO; PR:Q46817; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015208; F:guanine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0098710; P:guanine import across plasma membrane; IDA:EcoCyc.
DR GO; GO:0035344; P:hypoxanthine transport; IDA:EcoCyc.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR006043; NCS2.
DR PANTHER; PTHR43337; PTHR43337; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..455
FT /note="Guanine/hypoxanthine permease GhxQ"
FT /id="PRO_0000169358"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..65
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..103
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..115
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..186
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..260
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..320
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..336
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..366
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 392..427
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 455 AA; 46758 MW; B56EDA4AAA01C797 CRC64;
MSGDILQTPD APKPQGALDN YFKITARGST VRQEVLAGLT TFLAMVYSVI VVPGMLGKAG
FPPAAVFVAT CLVAGFGSLL MGLWANLPMA IGCAISLTAF TAFSLVLGQQ ISVPVALGAV
FLMGVIFTAI SVTGVRTWIL RNLPMGIAHG TGIGIGLFLL LIAANGVGMV IKNPIEGLPV
ALGAFTSFPV MMSLLGLAVI FGLEKCRVPG GILLVIIAIS IIGLIFDPAV KYHGLVAMPS
LTGEDGKSLI FSLDIMGALQ PTVLPSVLAL VMTAVFDATG TIRAVAGQAN LLDKDNQIIN
GGKALTSDSV SSIFSGLVGA APAAVYIESA AGTAAGGKTG LTATVVGALF LLILFLSPLS
FLIPGYATAP ALMYVGLLML SNVSKLDFND FIDAMAGLVC AVFIVLTCNI VTGIMLGFVT
LVVGRVFARE WQKLNIGTVI ITAALVAFYA GGWAI
