YDDG_STAND
ID YDDG_STAND Reviewed; 287 AA.
AC D7A5Q8;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Aromatic amino acid exporter YddG {ECO:0000305};
GN Name=yddG {ECO:0000303|PubMed:27281193};
GN OrderedLocusNames=Snov_2734 {ECO:0000312|EMBL:ADH90023.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Starkeya.
OX NCBI_TaxID=639283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
RN [2] {ECO:0007744|PDB:5I20}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, DOMAIN, AND MUTAGENESIS OF TYR-78; HIS-79; TYR-82; TRP-101 AND
RP TRP-163.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
RX PubMed=27281193; DOI=10.1038/nature17991;
RA Tsuchiya H., Doki S., Takemoto M., Ikuta T., Higuchi T., Fukui K.,
RA Usuda Y., Tabuchi E., Nagatoishi S., Tsumoto K., Nishizawa T., Ito K.,
RA Dohmae N., Ishitani R., Nureki O.;
RT "Structural basis for amino acid export by DMT superfamily transporter
RT YddG.";
RL Nature 534:417-420(2016).
CC -!- FUNCTION: Amino acid transporter with broad substrate specificity
CC (PubMed:27281193). Can transport various amino acids, including L-
CC threonine, L-methionine, L-lysine and L-glutamate (PubMed:27281193).
CC {ECO:0000269|PubMed:27281193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine(in) = L-threonine(out); Xref=Rhea:RHEA:35019,
CC ChEBI:CHEBI:57926; Evidence={ECO:0000305|PubMed:27281193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939,
CC ChEBI:CHEBI:57844; Evidence={ECO:0000305|PubMed:27281193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935,
CC ChEBI:CHEBI:32551; Evidence={ECO:0000305|PubMed:27281193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000305|PubMed:27281193};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:27281193}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27281193}.
CC -!- DOMAIN: The overall structure is basket-shaped, with a large substrate-
CC binding cavity at the center of the molecule, and is composed of
CC inverted structural repeats related by two-fold pseudo-symmetry. The
CC central cavity functions as the binding site for a wide range of
CC substrates. {ECO:0000269|PubMed:27281193}.
CC -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC superfamily. Aromatic amino acid/paraquat exporter (ArAA/P-E) (TC
CC 2.A.7.17) family. {ECO:0000305}.
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DR EMBL; CP002026; ADH90023.1; -; Genomic_DNA.
DR RefSeq; WP_013167527.1; NC_014217.1.
DR PDB; 5I20; X-ray; 2.40 A; A/B/C/D/E/F=1-287.
DR PDBsum; 5I20; -.
DR SMR; D7A5Q8; -.
DR TCDB; 2.A.7.3.66; the drug/metabolite transporter (dmt) superfamily.
DR EnsemblBacteria; ADH90023; ADH90023; Snov_2734.
DR KEGG; sno:Snov_2734; -.
DR eggNOG; COG0697; Bacteria.
DR HOGENOM; CLU_067094_0_0_5; -.
DR OMA; GIFGYHA; -.
DR OrthoDB; 1515911at2; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR000620; EamA_dom.
DR Pfam; PF00892; EamA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..287
FT /note="Aromatic amino acid exporter YddG"
FT /id="PRO_5003092348"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 25..31
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 55..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 87..90
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 112..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 140..149
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 171..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 199..208
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 209..233
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 234..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 237..258
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 259..264
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT TOPO_DOM 285..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27281193,
FT ECO:0007744|PDB:5I20"
FT DOMAIN 7..136
FT /note="EamA 1"
FT /evidence="ECO:0000255"
FT DOMAIN 151..281
FT /note="EamA 2"
FT /evidence="ECO:0000255"
FT MUTAGEN 78
FT /note="Y->A: Shows moderate effects on the transport
FT activities of both threonine and methionine."
FT /evidence="ECO:0000269|PubMed:27281193"
FT MUTAGEN 79
FT /note="H->A: Abolishes the transport activities for both
FT threonine and methionine."
FT /evidence="ECO:0000269|PubMed:27281193"
FT MUTAGEN 82
FT /note="Y->A: Enhances methionine transport and slightly
FT reduces threonine transport."
FT /evidence="ECO:0000269|PubMed:27281193"
FT MUTAGEN 101
FT /note="W->A: Exhibits decreased transport activity for
FT threonine, but not for methionine."
FT /evidence="ECO:0000269|PubMed:27281193"
FT MUTAGEN 163
FT /note="W->A: Exhibits decreased transport activity for
FT threonine, but not for methionine."
FT /evidence="ECO:0000269|PubMed:27281193"
SQ SEQUENCE 287 AA; 29452 MW; DD2D954805112C8E CRC64;
MSRSSATLIG FTAILLWSTL ALATSSTGAV PPFLLTALTF TIGGAVGIAA GLARGVGLSV
LRQPWPVWVH GIGGLFGYHF FYFSALKLAP PAEAGLVAYL WPLLIVLFSA FLPGERLRPA
HVAGALMGLA GTVVLLGARA GGFGFAPEYV PGYLAAAACA VIWSVYSVAS RRFARVPTEV
VAGFCLATAA LSALCHILFE PSVWPVGSEW LAVVALGIGP VGIAFYTWDI GMKRGDVRLL
GVLSYAAPVL STLLLVVAGF AAPSGALAIA CALIVGGAAV ATLLARR
