AMT1_ARCFU
ID AMT1_ARCFU Reviewed; 391 AA.
AC O29285;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Ammonium transporter Amt1 {ECO:0000303|PubMed:16511180};
DE AltName: Full=Af-Amt1 {ECO:0000303|PubMed:24958855};
GN Name=amt1 {ECO:0000303|PubMed:16511180};
GN OrderedLocusNames=AF_0977 {ECO:0000312|EMBL:AAB90264.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, AND CRYSTALLIZATION.
RX PubMed=16511180; DOI=10.1107/s1744309105027004;
RA Andrade S.L., Dickmanns A., Ficner R., Einsle O.;
RT "Expression, purification and crystallization of the ammonium transporter
RT Amt-1 from Archaeoglobus fulgidus.";
RL Acta Crystallogr. F 61:861-863(2005).
RN [3]
RP FUNCTION, AND THERMODYNAMICS.
RX PubMed=22804733; DOI=10.1021/jp305440f;
RA Ullmann R.T., Andrade S.L., Ullmann G.M.;
RT "Thermodynamics of transport through the ammonium transporter Amt-1
RT investigated with free energy calculations.";
RL J. Phys. Chem. B 116:9690-9703(2012).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24958855; DOI=10.1073/pnas.1406409111;
RA Wacker T., Garcia-Celma J.J., Lewe P., Andrade S.L.;
RT "Direct observation of electrogenic NH4(+) transport in ammonium transport
RT (Amt) proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9995-10000(2014).
RN [5] {ECO:0007744|PDB:2B2F, ECO:0007744|PDB:2B2H, ECO:0007744|PDB:2B2I, ECO:0007744|PDB:2B2J}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=16214888; DOI=10.1073/pnas.0506254102;
RA Andrade S.L., Dickmanns A., Ficner R., Einsle O.;
RT "Crystal structure of the archaeal ammonium transporter Amt-1 from
RT Archaeoglobus fulgidus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14994-14999(2005).
CC -!- FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3))
CC (PubMed:22804733, PubMed:24958855). Transport is electrogenic
CC (PubMed:22804733, PubMed:24958855). Transport the ammonium and
CC methylammonium cation with high specificity (PubMed:24958855).
CC {ECO:0000269|PubMed:22804733, ECO:0000269|PubMed:24958855}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Transport is pH-dependent, with a steep decline at pH values about
CC 5.0. {ECO:0000269|PubMed:24958855};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16214888,
CC ECO:0000269|PubMed:16511180}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16214888,
CC ECO:0000269|PubMed:16511180}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16214888}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
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DR EMBL; AE000782; AAB90264.1; -; Genomic_DNA.
DR PIR; A69372; A69372.
DR RefSeq; WP_010878477.1; NC_000917.1.
DR PDB; 2B2F; X-ray; 1.72 A; A=1-391.
DR PDB; 2B2H; X-ray; 1.54 A; A=1-391.
DR PDB; 2B2I; X-ray; 1.85 A; A=1-391.
DR PDB; 2B2J; X-ray; 1.85 A; A=1-391.
DR PDBsum; 2B2F; -.
DR PDBsum; 2B2H; -.
DR PDBsum; 2B2I; -.
DR PDBsum; 2B2J; -.
DR AlphaFoldDB; O29285; -.
DR SMR; O29285; -.
DR STRING; 224325.AF_0977; -.
DR TCDB; 1.A.11.1.6; the ammonium transporter channel (amt) family.
DR EnsemblBacteria; AAB90264; AAB90264; AF_0977.
DR GeneID; 24794578; -.
DR KEGG; afu:AF_0977; -.
DR eggNOG; arCOG04397; Archaea.
DR HOGENOM; CLU_000445_33_0_2; -.
DR OMA; PHNVPFI; -.
DR OrthoDB; 66605at2157; -.
DR PhylomeDB; O29285; -.
DR EvolutionaryTrace; O29285; -.
DR Proteomes; UP000002199; 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:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR PANTHER; PTHR43029; PTHR43029; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR TIGRFAMs; TIGR00836; amt; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ammonia transport; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..391
FT /note="Ammonium transporter Amt1"
FT /id="PRO_0000453005"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 8..27
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 28..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 58..89
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 90..106
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 107..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 114..137
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 138..152
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 153..170
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 171..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 209..217
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 238..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 246..263
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 264..268
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 288..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 320..337
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16214888"
FT TRANSMEM 338..363
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16214888"
FT TOPO_DOM 364..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16214888"
FT SITE 157
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT SITE 305
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT HELIX 3..28
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 36..56
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:2B2H"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2B2H"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 85..104
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2B2H"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2B2H"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:2B2H"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 187..206
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2B2H"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 214..241
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:2B2H"
FT TURN 261..266
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 269..292
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 301..319
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 335..366
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:2B2H"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:2B2H"
SQ SEQUENCE 391 AA; 40992 MW; 04005B139865A546 CRC64;
MSDGNVAWIL ASTALVMLMV PGVGFFYAGM VRRKNAVNMI ALSFISLIIT VLLWIFYGYS
VSFGNDISGI IGGLNYALLS GVKGEDLLFM MYQMMFAAVT IAILTSAIAE RAKVSSFILL
SALWLTFVYA PFAHWLWGGG WLAKLGALDF AGGMVVHISS GFAALAVAMT IGKRAGFEEY
SIEPHSIPLT LIGAALLWFG WFGFNGGSAL AANDVAINAV VVTNTSAAVA GFVWMVIGWI
KGKPGSLGIV SGAIAGLAAI TPAAGFVDVK GAIVIGLVAG IVCYLAMDFR IKKKIDESLD
AWAIHGIGGL WGSVAVGILA NPEVNGYAGL LFGNPQLLVS QLIAVASTTA YAFLVTLILA
KAVDAAVGLR VSSQEEYVGL DLSQHEEVAY T
