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Protein

Glutamate transporter homolog

Gene

PH1295

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref. 11). Has only very low glutamate transport activity (PubMed:19380583, PubMed:17230192). Functions as a symporter that transports one amino acid molecule together with two or three Na+ ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref. 11). Na+ binding enhances the affinity for aspartate (PubMed:19380583, Ref. 11). Mediates Cl- flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na+ symport (PubMed:17435767). In contrast to mammalian homologs, transport does not depend on pH or K+ ions (PubMed:19380583).4 Publications

Kineticsi

  1. KM=120 nM for L-aspartate transport1 Publication
  1. Vmax=3.7 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi306Sodium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi308Sodium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi310Sodium 1Combined sources1 Publication1
Binding sitei314AspartateCombined sources1 Publication1
Metal bindingi352Sodium 2; via carbonyl oxygenCombined sources1 Publication1
Binding sitei355Aspartate; via carbonyl oxygenCombined sources1 Publication1
Binding sitei394AspartateCombined sources1 Publication1
Metal bindingi401Sodium 1; via carbonyl oxygenCombined sources1 Publication1
Binding sitei401AspartateCombined sources1 Publication1
Metal bindingi405Sodium 1Combined sources1 Publication1

GO - Molecular functioni

  • chloride transmembrane transporter activity Source: UniProtKB
  • L-aspartate transmembrane transporter activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • sodium:amino acid symporter activity Source: UniProtKB

GO - Biological processi

  • chloride transmembrane transport Source: UniProtKB
  • L-aspartate import across plasma membrane Source: UniProtKB
  • L-aspartate transmembrane transport Source: UniProtKB
  • protein homotrimerization Source: UniProtKB

Keywordsi

Biological processAmino-acid transport, Symport, Transport
LigandChloride, Metal-binding, Sodium

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1291-MONOMER.

Protein family/group databases

TCDBi2.A.23.1.5. the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate transporter homolog1 Publication
Short name:
Glt(Ph)1 Publication
Alternative name(s):
Sodium-aspartate symporter Glt(Ph)1 Publication
Sodium-dependent aspartate transporter2 Publications
Gene namesi
Ordered Locus Names:PH1295Imported
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11Cytoplasmic1 PublicationAdd BLAST11
Transmembranei12 – 30Helical; Name=11 PublicationAdd BLAST19
Topological domaini31 – 41Extracellular1 PublicationAdd BLAST11
Transmembranei42 – 62Helical; Name=21 PublicationAdd BLAST21
Topological domaini63 – 80Cytoplasmic1 PublicationAdd BLAST18
Transmembranei81 – 103Helical; Name=31 PublicationAdd BLAST23
Topological domaini104 – 121Extracellular1 PublicationAdd BLAST18
Transmembranei122 – 160Discontinuously helical; Name=41 PublicationAdd BLAST39
Topological domaini161 – 196Cytoplasmic1 PublicationAdd BLAST36
Transmembranei197 – 218Helical; Name=51 PublicationAdd BLAST22
Topological domaini219 – 230Extracellular1 PublicationAdd BLAST12
Transmembranei231 – 251Helical; Name=61 PublicationAdd BLAST21
Topological domaini252 – 260Cytoplasmic1 Publication9
Intramembranei261 – 289Discontinuously helical1 PublicationAdd BLAST29
Topological domaini290 – 297Cytoplasmic1 Publication8
Transmembranei298 – 320Discontinuously helical; Name=71 PublicationAdd BLAST23
Topological domaini321 – 337Extracellular1 PublicationAdd BLAST17
Intramembranei338 – 372Discontinuously helical1 PublicationAdd BLAST35
Topological domaini373 – 391Extracellular1 PublicationAdd BLAST19
Transmembranei392 – 412Helical; Name=81 PublicationAdd BLAST21
Topological domaini413 – 425Cytoplasmic1 PublicationAdd BLAST13

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65S → V: Strongly decreased chloride conductance. 1 Publication1
Mutagenesisi276R → S: Increased rate of aspartate transport; when associated with R-395. 1 Publication1
Mutagenesisi311M → A: Decreased dependence of aspartate binding on Na(+) concentration. 1 Publication1
Mutagenesisi395M → R: Increased rate of aspartate transport; when associated with S-276. 1 Publication1
Mutagenesisi397R → A: Strongly decreased affinity for aspartate. 1 Publication1
Mutagenesisi405D → N: Strongly decreased affinity for aspartate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004408931 – 425Glutamate transporter homologAdd BLAST425

Interactioni

Subunit structurei

Homotrimer.8 Publications

Protein-protein interaction databases

DIPiDIP-59313N.
STRINGi70601.PH1295.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XFHX-ray3.50A/B/C1-417[»]
2NWLX-ray2.96A/B/C1-417[»]
2NWWX-ray3.20A/B/C1-417[»]
2NWXX-ray3.29A/B/C1-417[»]
3KBCX-ray3.51A/B/C1-425[»]
3V8FX-ray3.80A/B/C1-417[»]
3V8GX-ray4.66A/B/C/D/E/F1-417[»]
4IZMX-ray4.50A/B/C1-417[»]
4OYEX-ray4.00A/B/C/D/E/F/G/H/I/J/K/L8-416[»]
4OYFX-ray3.41A/B/C/D/E/F1-419[»]
4P19X-ray3.25A/B/C1-417[»]
4P1AX-ray3.75A/B/C1-417[»]
4P3JX-ray3.50A/B/C1-417[»]
4P6HX-ray4.08A/B/C1-417[»]
4X2SX-ray4.21A/B/C1-417[»]
5CFYX-ray3.50A/B/C/D/E/F1-425[»]
ProteinModelPortaliO59010.
SMRiO59010.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59010.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni276 – 278Aspartate bindingCombined sources1 Publication3

Domaini

Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, regions involved in trimerization do not move.6 Publications

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG04335. Archaea.
COG1301. LUCA.
HOGENOMiHOG000208778.
OMAiVMGISEM.
OrthoDBiPOG093Z02C3.

Family and domain databases

Gene3Di1.10.3860.10. 1 hit.
InterProiView protein in InterPro
IPR001991. Na-dicarboxylate_symporter.
IPR018107. Na-dicarboxylate_symporter_CS.
PfamiView protein in Pfam
PF00375. SDF. 1 hit.
PRINTSiPR00173. EDTRNSPORT.
SUPFAMiSSF118215. SSF118215. 1 hit.
PROSITEiView protein in PROSITE
PS00713. NA_DICARBOXYL_SYMP_1. 1 hit.

Sequencei

Sequence statusi: Complete.

O59010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLYRKYIEY PVLQKILIGL ILGAIVGLIL GHYGYADAVK TYVKPFGDLF
60 70 80 90 100
VRLLKMLVMP IVFASLVVGA ASISPARLGR VGVKIVVYYL LTSAFAVTLG
110 120 130 140 150
IIMARLFNPG AGIHLAVGGQ QFQPKQAPPL VKILLDIVPT NPFGALANGQ
160 170 180 190 200
VLPTIFFAII LGIAITYLMN SENEKVRKSA ETLLDAINGL AEAMYKIVNG
210 220 230 240 250
VMQYAPIGVF ALIAYVMAEQ GVKVVGELAK VTAAVYVGLT LQILLVYFVL
260 270 280 290 300
LKIYGIDPIS FIKKAKDAML TAFVTRSSSG TLPVTMRVAK EMGISEGIYS
310 320 330 340 350
FTLPLGATIN MDGTALYQGV CTFFIANALG SHLTVGQQLT IVLTAVLASI
360 370 380 390 400
GTAGVPGAGA IMLAMVLESV GLPLTDPNVA AAYAMILGID AILDMGRTMV
410 420
NVTGDLTGTA IVAKTEGELE KGVIA
Length:425
Mass (Da):44,807
Last modified:August 1, 1998 - v1
Checksum:i2F32EC45B0212FF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30399.1.
PIRiE71075.

Genome annotation databases

EnsemblBacteriaiBAA30399; BAA30399; BAA30399.
KEGGipho:PH1295.

Similar proteinsi

Entry informationi

Entry nameiGLT_PYRHO
AccessioniPrimary (citable) accession number: O59010
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2017
Last sequence update: August 1, 1998
Last modified: August 30, 2017
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families