GLNK3_ARCFU
ID GLNK3_ARCFU Reviewed; 120 AA.
AC O28524;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nitrogen regulatory protein GlnK3 {ECO:0000305};
GN Name=glnK3 {ECO:0000303|PubMed:22039461};
GN OrderedLocusNames=AF_1750 {ECO:0000312|EMBL:AAB89500.1};
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] {ECO:0007744|PDB:3T9Z, ECO:0007744|PDB:3TA0, ECO:0007744|PDB:3TA1, ECO:0007744|PDB:3TA2}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 12-120 IN COMPLEXES WITH
RP 2-OXOGLUTARATE; ADP AND ATP, FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF PHE-97.
RX PubMed=22039461; DOI=10.1371/journal.pone.0026327;
RA Maier S., Schleberger P., Lu W., Wacker T., Pfluger T., Litz C.,
RA Andrade S.L.;
RT "Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing
RT of 2-oxoglutarate.";
RL PLoS ONE 6:e26327-e26327(2011).
CC -!- FUNCTION: Involved in the regulation of nitrogen metabolism (By
CC similarity). Regulates the activity of its targets by protein-protein
CC interaction in response to the nitrogen status of the cell (By
CC similarity). Regulates the activity of the ammonia channel Amt3 via
CC direct interaction (Probable). {ECO:0000250|UniProtKB:Q60381,
CC ECO:0000305|PubMed:22039461}.
CC -!- ACTIVITY REGULATION: Activity is influenced by intracellular pools of
CC the effector molecules ATP, ADP and 2-oxoglutarate. It senses the
CC cellular nitrogen status through 2-oxoglutarate, and the energy level
CC of the cell by binding both ATP and ADP with different affinities. ATP
CC and 2-oxoglutarate prohibit binding to Amt3. ADP promotes the complex
CC formation. {ECO:0000269|PubMed:22039461}.
CC -!- SUBUNIT: Homotrimer (PubMed:22039461). Interacts and forms a complex
CC with Amt3 (By similarity). {ECO:0000250|UniProtKB:Q60381,
CC ECO:0000269|PubMed:22039461}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8ZYW0}.
CC -!- DOMAIN: Undergoes conformational changes upon binding of effector
CC molecules. {ECO:0000269|PubMed:22039461}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AE000782; AAB89500.1; -; Genomic_DNA.
DR PIR; E69468; E69468.
DR PDB; 3T9Z; X-ray; 1.82 A; A/B/C/D/E/F=12-120.
DR PDB; 3TA0; X-ray; 2.30 A; A/B/C/D/E/F=12-120.
DR PDB; 3TA1; X-ray; 1.90 A; A/B/C/D/E/F=12-120.
DR PDB; 3TA2; X-ray; 1.90 A; A/B/C=12-120.
DR PDBsum; 3T9Z; -.
DR PDBsum; 3TA0; -.
DR PDBsum; 3TA1; -.
DR PDBsum; 3TA2; -.
DR AlphaFoldDB; O28524; -.
DR SMR; O28524; -.
DR STRING; 224325.AF_1750; -.
DR EnsemblBacteria; AAB89500; AAB89500; AF_1750.
DR KEGG; afu:AF_1750; -.
DR eggNOG; arCOG02305; Archaea.
DR HOGENOM; CLU_082268_0_1_2; -.
DR OMA; YRGTEHV; -.
DR PhylomeDB; O28524; -.
DR EvolutionaryTrace; O28524; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002187; N-reg_PII.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR017918; N-reg_PII_CS.
DR PANTHER; PTHR30115; PTHR30115; 1.
DR Pfam; PF00543; P-II; 1.
DR PRINTS; PR00340; PIIGLNB.
DR SMART; SM00938; P-II; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR PROSITE; PS00638; PII_GLNB_CTER; 1.
DR PROSITE; PS51343; PII_GLNB_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..120
FT /note="Nitrogen regulatory protein GlnK3"
FT /id="PRO_0000453014"
FT BINDING 40
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA1"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA0, ECO:0007744|PDB:3TA2"
FT BINDING 48..52
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA2"
FT BINDING 48..50
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA1"
FT BINDING 48..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA0, ECO:0007744|PDB:3TA2"
FT BINDING 69
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA2"
FT BINDING 75
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA1"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA0, ECO:0007744|PDB:3TA2"
FT BINDING 98..101
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA1"
FT BINDING 98..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA0, ECO:0007744|PDB:3TA2"
FT BINDING 98
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:22039461,
FT ECO:0007744|PDB:3TA2"
FT MUTAGEN 97
FT /note="F->I,P: Retains the ability to bind 2-oxoglutarate."
FT /evidence="ECO:0000269|PubMed:22039461"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3T9Z"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3T9Z"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:3T9Z"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:3T9Z"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3TA2"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3TA2"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:3T9Z"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3T9Z"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:3T9Z"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3T9Z"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3T9Z"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3T9Z"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3T9Z"
SQ SEQUENCE 120 AA; 13456 MW; FD5A76FAE9011E8E CRC64;
MRRLPTREVV DMKMVVAVIR PEKLECVKKA LEERGFVGMT VTEVKGRGEQ KGIRLQFRGR
EVEVDLLQKT KVEVVVSDDA VDEVVEAIVS SARTGKFGDG RIFVIPVEKS VKIRTGDEEV
