DGOT_ECOLI
ID DGOT_ECOLI Reviewed; 430 AA.
AC P0AA76; P31457; Q2M803;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=D-galactonate transporter {ECO:0000303|PubMed:31083648};
DE AltName: Full=D-galactonate/H(+) symporter {ECO:0000303|PubMed:31083648};
GN Name=dgoT {ECO:0000303|PubMed:211976}; Synonyms=yidT;
GN OrderedLocusNames=b3691, JW5859;
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=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
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 [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, AND OPERON.
RC STRAIN=K12;
RX PubMed=211976; DOI=10.1007/bf00415730;
RA Cooper R.A.;
RT "The utilisation of D-galactonate and D-2-oxo-3-deoxygalactonate by
RT Escherichia coli K-12. Biochemical and genetical studies.";
RL Arch. Microbiol. 118:199-206(1978).
RN [5]
RP SIMILARITY TO DAL5 FAMILY.
RA Koonin E.V.;
RL Unpublished observations (OCT-1993).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION, INDUCTION, OPERON, AND DISRUPTION PHENOTYPE.
RX PubMed=30455279; DOI=10.1128/jb.00281-18;
RA Singh B., Arya G., Kundu N., Sangwan A., Nongthombam S., Chaba R.;
RT "Molecular and functional insights into the regulation of D-galactonate
RT metabolism by the transcriptional regulator DgoR in Escherichia coli.";
RL J. Bacteriol. 201:e00281-e00281(2019).
RN [8] {ECO:0007744|PDB:6E9N, ECO:0007744|PDB:6E9O}
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF WILD-TYPE AND MUTANT GLN-118 IN
RP COMPLEX WITH D-GALACTONATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY,
RP DOMAIN, PROPOSED TRANSPORT MECHANISM, AND MUTAGENESIS OF ASP-31 AND
RP GLU-118.
RX PubMed=31083648; DOI=10.1371/journal.pbio.3000260;
RA Leano J.B., Batarni S., Eriksen J., Juge N., Pak J.E., Kimura-Someya T.,
RA Robles-Colmenares Y., Moriyama Y., Stroud R.M., Edwards R.H.;
RT "Structures suggest a mechanism for energy coupling by a family of organic
RT anion transporters.";
RL PLoS Biol. 17:e3000260-e3000260(2019).
CC -!- FUNCTION: Involved in D-galactonate metabolism (PubMed:211976,
CC PubMed:30455279). Catalyzes the proton-dependent uptake of galactonate
CC into the cell (PubMed:31083648). {ECO:0000269|PubMed:211976,
CC ECO:0000269|PubMed:30455279, ECO:0000269|PubMed:31083648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactonate(in) + H(+)(in) = D-galactonate(out) + H(+)(out);
CC Xref=Rhea:RHEA:29835, ChEBI:CHEBI:12931, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:31083648};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29837;
CC Evidence={ECO:0000269|PubMed:31083648};
CC -!- ACTIVITY REGULATION: Uptake is inhibited by the proton ionophore
CC nigericin, which dissipates the proton gradient, and by the potassium
CC ionophore valinomycin, which dissipates the membrane potential.
CC {ECO:0000269|PubMed:31083648}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for D-galactonate {ECO:0000269|PubMed:31083648};
CC Vmax=1.94 nmol/min/ug enzyme {ECO:0000269|PubMed:31083648};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:31083648}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:31083648}.
CC -!- INDUCTION: Part of the dgoRKADT operon, which encodes proteins for the
CC metabolism of D-galactonate (PubMed:211976, PubMed:30455279).
CC Negatively regulated by DgoR (PubMed:30455279). Expression is induced
CC in the presence of D-galactonate (PubMed:30455279).
CC {ECO:0000269|PubMed:211976, ECO:0000269|PubMed:30455279}.
CC -!- DOMAIN: Major conformational changes and local movement around the
CC substrate site occur to accommodate substrate for transport
CC (PubMed:31083648). Active transport requires reversible protonation of
CC both Asp-31 and Glu-118 (PubMed:31083648).
CC {ECO:0000269|PubMed:31083648}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant cannot grow on D-galactonate.
CC {ECO:0000269|PubMed:30455279}.
CC -!- MISCELLANEOUS: The exact stoichiometry of cotransport is not determined
CC and could be greater than 1. {ECO:0000269|PubMed:31083648}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62043.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L10328; AAA62043.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76714.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77603.1; -; Genomic_DNA.
DR PIR; D65171; D65171.
DR RefSeq; NP_418146.4; NC_000913.3.
DR PDB; 6E9N; X-ray; 2.92 A; A/B=1-430.
DR PDB; 6E9O; X-ray; 3.50 A; A/B=1-430.
DR PDBsum; 6E9N; -.
DR PDBsum; 6E9O; -.
DR AlphaFoldDB; P0AA76; -.
DR SMR; P0AA76; -.
DR BioGRID; 4263278; 7.
DR DIP; DIP-9436N; -.
DR STRING; 511145.b3691; -.
DR TCDB; 2.A.1.14.7; the major facilitator superfamily (mfs).
DR PaxDb; P0AA76; -.
DR PRIDE; P0AA76; -.
DR EnsemblBacteria; AAC76714; AAC76714; b3691.
DR EnsemblBacteria; BAE77603; BAE77603; BAE77603.
DR GeneID; 948196; -.
DR KEGG; ecj:JW5859; -.
DR KEGG; eco:b3691; -.
DR PATRIC; fig|511145.12.peg.3814; -.
DR EchoBASE; EB1666; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR InParanoid; P0AA76; -.
DR OMA; RVVTTWF; -.
DR PhylomeDB; P0AA76; -.
DR BioCyc; EcoCyc:YIDT-MON; -.
DR BioCyc; MetaCyc:YIDT-MON; -.
DR PRO; PR:P0AA76; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042881; F:D-galactonate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0034194; P:D-galactonate catabolic process; IMP:EcoCyc.
DR GO; GO:0042875; P:D-galactonate transmembrane transport; IDA:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..430
FT /note="D-galactonate transporter"
FT /id="PRO_0000121377"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 18..39
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 40..50
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 75..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 101..103
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 104..125
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 126..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 165..168
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 191..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 242..267
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 268..276
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 298..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 334..336
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 337..354
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 355..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 396..400
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9N"
FT TOPO_DOM 424..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:31083648, ECO:0007744|PDB:6E9N"
FT BINDING 29
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9O"
FT BINDING 32
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9O"
FT BINDING 64
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9O"
FT BINDING 358
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000269|PubMed:31083648,
FT ECO:0007744|PDB:6E9O"
FT SITE 31
FT /note="Important for transport activity"
FT /evidence="ECO:0000305|PubMed:31083648"
FT SITE 118
FT /note="Important for transport activity"
FT /evidence="ECO:0000305|PubMed:31083648"
FT MUTAGEN 31
FT /note="D->N: Loss of galactonate transport activity."
FT /evidence="ECO:0000269|PubMed:31083648"
FT MUTAGEN 118
FT /note="E->Q: Loss of galactonate transport activity."
FT /evidence="ECO:0000269|PubMed:31083648"
SQ SEQUENCE 430 AA; 47077 MW; 86B1902777F2E461 CRC64;
MDIPVNAAKP GRRRYLTLVM IFITVVICYV DRANLAVASA HIQEEFGITK AEMGYVFSAF
AWLYTLCQIP GGWFLDRVGS RVTYFIAIFG WSVATLFQGF ATGLMSLIGL RAITGIFEAP
AFPTNNRMVT SWFPEHERAS AVGFYTSGQF VGLAFLTPLL IWIQEMLSWH WVFIVTGGIG
IIWSLIWFKV YQPPRLTKGI SKAELDYIRD GGGLVDGDAP VKKEARQPLT AKDWKLVFHR
KLIGVYLGQF AVASTLWFFL TWFPNYLTQE KGITALKAGF MTTVPFLAAF VGVLLSGWVA
DLLVRKGFSL GFARKTPIIC GLLISTCIMG ANYTNDPMMI MCLMALAFFG NGFASITWSL
VSSLAPMRLI GLTGGVFNFA GGLGGITVPL VVGYLAQGYG FAPALVYISA VALIGALSYI
LLVGDVKRVG
