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AMT3_ARCFU
ID   AMT3_ARCFU              Reviewed;         388 AA.
AC   O28525;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Ammonium transporter Amt3 {ECO:0000305};
DE   AltName: Full=Af-Amt3 {ECO:0000303|PubMed:24958855};
GN   Name=amt3 {ECO:0000305};
GN   OrderedLocusNames=AF_1749 {ECO:0000312|EMBL:AAB89501.1};
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   FUNCTION.
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).
CC   -!- FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3))
CC       (PubMed:24958855). Transport is electrogenic (PubMed:24958855).
CC       Transport the ammonium and methylammonium cation with high specificity
CC       (PubMed:24958855). {ECO:0000269|PubMed:24958855}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:O29285}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O29285};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC       family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89501.1; -; Genomic_DNA.
DR   PIR; D69468; D69468.
DR   RefSeq; WP_010879245.1; NC_000917.1.
DR   AlphaFoldDB; O28525; -.
DR   SMR; O28525; -.
DR   STRING; 224325.AF_1749; -.
DR   EnsemblBacteria; AAB89501; AAB89501; AF_1749.
DR   GeneID; 1484972; -.
DR   KEGG; afu:AF_1749; -.
DR   eggNOG; arCOG04397; Archaea.
DR   HOGENOM; CLU_000445_33_0_2; -.
DR   OMA; MACWNSN; -.
DR   OrthoDB; 66605at2157; -.
DR   PhylomeDB; O28525; -.
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; IPR018047; Ammonium_transpt_CS.
DR   InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR   PANTHER; PTHR43029; PTHR43029; 1.
DR   Pfam; PF00909; Ammonium_transp; 1.
DR   TIGRFAMs; TIGR00836; amt; 1.
DR   PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE   3: Inferred from homology;
KW   Ammonia transport; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..388
FT                   /note="Ammonium transporter Amt3"
FT                   /id="PRO_0000453007"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   388 AA;  40252 MW;  DD59F362FBBD8A8A CRC64;
     MQSGDISWLL ISTALVVLMT PALGLFYGGM VRAKNVLSTI TMCFVALAIV SVQWILLGYT
     IAFGDDVSGL TGNLVFIGLR NVSMSDYGFV AFQMAFAAIT LAIIVSALAE RVKLSAFLLF
     GILWTTFVYD PIAHWVWGGG WLAGIGALDF AGGTVVHISS GFSALALALL VGRRTGYGEY
     NIEPHNIPMT LLGTALLWFG WFGFNAGSAL EANDVALNAF LVTNTSAAMG ALSWMFASWL
     KGKPGSLGVA SGAIAGLVAI TPAAGYVDPL SALVIGGVAG VVCYAAMLLR VRAGVDESLD
     AWAVHGVGGL WGAIATGIFA SVGATGLVAG NAQQLLLQII AALVATAYAF LVTLILAKAV
     DAAVGLRVSS QEEYVGLDLS QHEEVAYT
 
 
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