ID AMT1_METJA Reviewed; 391 AA.
AC Q60366;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Ammonium transporter Amt1 {ECO:0000305};
GN Name=amt1 {ECO:0000303|PubMed:17203075}; OrderedLocusNames=MJ0058;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH GLNK1.
RX PubMed=17203075; DOI=10.1038/sj.emboj.7601492;
RA Yildiz O., Kalthoff C., Raunser S., Kuhlbrandt W.;
RT "Structure of GlnK1 with bound effectors indicates regulatory mechanism for
RT ammonia uptake.";
RL EMBO J. 26:589-599(2007).
CC -!- FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3))
CC (By similarity). Transport is electrogenic (By similarity).
CC {ECO:0000250|UniProtKB:O29285}.
CC -!- ACTIVITY REGULATION: Activity is regulated by the nitrogen regulatory
CC protein GlnK1 via direct interaction (PubMed:17203075). Formation of
CC the GlnK1/Amt1 complex is decreased in the presence of Mg-ATP or 2-
CC oxoglutarate. The presence of both effectors abolishes the formation of
CC the complex (PubMed:17203075). {ECO:0000269|PubMed:17203075}.
CC -!- SUBUNIT: Homotrimer (PubMed:17203075). Interacts and forms a complex
CC with GlnK1 (PubMed:17203075). {ECO:0000269|PubMed:17203075}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC 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; L77117; AAB98038.1; -; Genomic_DNA.
DR PIR; B64307; B64307.
DR AlphaFoldDB; Q60366; -.
DR SMR; Q60366; -.
DR STRING; 243232.MJ_0058; -.
DR PaxDb; 243232-MJ_0058; -.
DR EnsemblBacteria; AAB98038; AAB98038; MJ_0058.
DR KEGG; mja:MJ_0058; -.
DR eggNOG; arCOG04397; Archaea.
DR HOGENOM; CLU_000445_33_1_2; -.
DR InParanoid; Q60366; -.
DR PhylomeDB; Q60366; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.3430.10; Ammonium transporter AmtB like domains; 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 NCBIfam; TIGR00836; amt; 1.
DR PANTHER; PTHR11730; AMMONIUM TRANSPORTER; 1.
DR PANTHER; PTHR11730:SF6; AMMONIUM TRANSPORTER; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR SUPFAM; SSF111352; Ammonium transporter; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 1: Evidence at protein level;
KW Ammonia transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..391
FT /note="Ammonium transporter Amt1"
FT /id="PRO_0000139764"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 158
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
FT SITE 309
FT /note="Twin-His motif. Important for optimum substrate
FT conductance"
FT /evidence="ECO:0000250|UniProtKB:P69681"
SQ SEQUENCE 391 AA; 41153 MW; 33632A73849E1C9A CRC64;
MFEVKHMDGI DVFFFMWAAS LIFFMKAGFI ALEIGQFRAK NVSYHCVLKL LDLAAVFIAY
LFIGYGISYG FENIMPLITG TFDADLGAWW MKMVMFAAAA VTIITGGVAE RIKILPYFIG
ALIVGGILYP IVEHLVWGGG FANLGINFHD YAGSGAVHLF GGLVGLMAAY VLGPRIDKYI
NGKPQAIPGH NIPIAVLGAF ILAFGWYGFN IGSASGIANG VELASVAMAT TMALAGGIIG
GALSSRNDPL YTANGMCAGL VAVCSGVDLF TPIGAFIVGL LAGIQQPFTY KFIEEKLKID
DVCAIGPVHA MSGLIGVICA GIPFLLKADA VSKVSITGQI IGAIVIALIA IVGGLIIYKG
LDLTIGLRVS EEAEKVGLDT AILQTTAYSE E
//
