ID Q9HXM5_PSEAE Unreviewed; 489 AA. AC Q9HXM5; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 158. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; DE Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964}; DE Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964}; DE Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964}; DE EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; GN Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964, GN ECO:0000313|EMBL:AAG07157.1}; GN OrderedLocusNames=PA3770 {ECO:0000313|EMBL:AAG07157.1}; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG07157.1, ECO:0000313|Proteomes:UP000002438}; RN [1] {ECO:0000313|EMBL:AAG07157.1, ECO:0000313|Proteomes:UP000002438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438}; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K., RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H., RA Hancock R.E., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [2] {ECO:0007829|PDB:4AVF} RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS). RX PubMed=23295481; DOI=10.1107/S1744309112044739; RA Moynie L., Schnell R., McMahon S.A., Sandalova T., Boulkerou W.A., RA Schmidberger J.W., Alphey M., Cukier C., Duthie F., Kopec J., Liu H., RA Jacewicz A., Hunter W.N., Naismith J.H., Schneider G.; RT "The AEROPATH project targeting Pseudomonas aeruginosa: crystallographic RT studies for assessment of potential targets in early-stage drug RT discovery."; RL Acta Crystallogr. F Struct. Biol. Commun. 69:25-34(2013). RN [3] {ECO:0007829|PDB:3ZFH} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=23519796; DOI=10.1107/S1744309113002352; RA Rao V.A., Shepherd S.M., Owen R., Hunter W.N.; RT "Structure of Pseudomonas aeruginosa inosine 5'-monophosphate RT dehydrogenase."; RL Acta Crystallogr. F Struct. Biol. Commun. 69:243-247(2013). RN [4] {ECO:0007829|PDB:4DQW} RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH ATP AND MN(2+). RX PubMed=23643948; DOI=10.1016/j.str.2013.03.011; RA Labesse G., Alexandre T., Vaupre L., Salard-Arnaud I., Him J.L., Raynal B., RA Bron P., Munier-Lehmann H.; RT "MgATP regulates allostery and fiber formation in IMPDHs."; RL Structure 21:975-985(2013). RN [5] {ECO:0007829|PDB:5AHL, ECO:0007829|PDB:5AHM} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IMP AND MG(2+). RX PubMed=26327379; DOI=10.1107/S1399004715013115; RA Labesse G., Alexandre T., Gelin M., Haouz A., Munier-Lehmann H.; RT "Crystallographic studies of two variants of Pseudomonas aeruginosa IMPDH RT with impaired allosteric regulation."; RL Acta Crystallogr. D 71:1890-1899(2015). RN [6] {ECO:0007829|PDB:6GJV, ECO:0007829|PDB:6GK9} RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS). RX PubMed=30769241; DOI=10.1016/j.ejmech.2019.01.064; RA Alexandre T., Lupan A., Helynck O., Vichier-Guerre S., Dugue L., Gelin M., RA Haouz A., Labesse G., Munier-Lehmann H.; RT "First-in-class allosteric inhibitors of bacterial IMPDHs."; RL Eur. J. Med. Chem. 167:124-132(2019). RN [7] {ECO:0007829|PDB:7QBJ, ECO:0007829|PDB:7QDX} RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-4 AND 92-203 IN COMPLEX WITH RP ATP AND MG(2+). RX PubMed=37338125; DOI=10.1002/pro.4703; RA Gedeon A., Ayoub N., Brule S., Raynal B., Karimova G., Gelin M., RA Mechaly A., Haouz A., Labesse G., Munier-Lehmann H.; RT "Insight into the role of the Bateman domain at the molecular and RT physiological levels through engineered IMP dehydrogenases."; RL Protein Sci. 32:e4703-e4703(2023). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to CC xanthosine 5'-phosphate (XMP), the first committed and rate-limiting CC step in the de novo synthesis of guanine nucleotides, and therefore CC plays an important role in the regulation of cell growth. CC {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; CC EC=1.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00024264, CC ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|ARBA:ARBA00001958, ECO:0000256|HAMAP- CC Rule:MF_01964}; CC -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme conformation by CC binding to the same site as the amobile flap. In contrast, mizoribine CC monophosphate (MZP) is a competitive inhibitor that induces the closed CC conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor CC inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of CC bacterial IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964, CC ECO:0000256|RuleBase:RU003928}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- INTERACTION: CC Q9HXM5; Q9HXM5: guaB; NbExp=5; IntAct=EBI-16056797, EBI-16056797; CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_01964, CC ECO:0000256|RuleBase:RU003927}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG07157.1; -; Genomic_DNA. DR PIR; H83173; H83173. DR RefSeq; NP_252459.1; NC_002516.2. DR RefSeq; WP_003092702.1; NZ_QZGE01000001.1. DR PDB; 3ZFH; X-ray; 2.25 A; A=1-489. DR PDB; 4AVF; X-ray; 2.23 A; A/B/C/D=1-489. DR PDB; 4DQW; X-ray; 2.51 A; A/B=1-489. DR PDB; 5AHL; X-ray; 1.95 A; A=1-489. DR PDB; 5AHM; X-ray; 1.74 A; A/B=1-489. DR PDB; 5AHN; X-ray; 1.65 A; A=1-489. DR PDB; 6GJV; X-ray; 2.11 A; A/B/C/D/E/F/G/H=1-489. DR PDB; 6GK9; X-ray; 2.54 A; A/B/C/D/E/F/G/H=1-489. DR PDB; 7QBJ; X-ray; 2.27 A; A/B/C/D=1-4, A/B/C/D=92-203. DR PDB; 7QDX; X-ray; 2.90 A; A/B=1-4, A/B=92-203. DR PDB; 7QEM; X-ray; 3.09 A; A/B/C/D=1-4, A/B/C/D=92-203. DR PDBsum; 3ZFH; -. DR PDBsum; 4AVF; -. DR PDBsum; 4DQW; -. DR PDBsum; 5AHL; -. DR PDBsum; 5AHM; -. DR PDBsum; 5AHN; -. DR PDBsum; 6GJV; -. DR PDBsum; 6GK9; -. DR AlphaFoldDB; Q9HXM5; -. DR SMR; Q9HXM5; -. DR DIP; DIP-60162N; -. DR STRING; 208964.PA3770; -. DR BindingDB; Q9HXM5; -. DR ChEMBL; CHEMBL4523953; -. DR PaxDb; 208964-PA3770; -. DR GeneID; 77219735; -. DR GeneID; 880535; -. DR KEGG; pae:PA3770; -. DR PATRIC; fig|208964.12.peg.3947; -. DR PseudoCAP; PA3770; -. DR HOGENOM; CLU_022552_2_2_6; -. DR InParanoid; Q9HXM5; -. DR OrthoDB; 9805398at2; -. DR PhylomeDB; Q9HXM5; -. DR BioCyc; PAER208964:G1FZ6-3841-MONOMER; -. DR BRENDA; 1.1.1.205; 5087. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central. DR CDD; cd04601; CBS_pair_IMPDH; 1. DR CDD; cd00381; IMPDH; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR046342; CBS_dom_sf. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR NCBIfam; TIGR01302; IMP_dehydrog; 1. DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM01240; IMPDH; 1. DR SUPFAM; SSF54631; CBS-domain pair; 1. DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3ZFH, ECO:0007829|PDB:4AVF}; KW ATP-binding {ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX}; KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE- KW ProRule:PRU00703}; KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP- KW Rule:MF_01964}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01964}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01964}; KW Nucleotide-binding {ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003927}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01964}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01964}; Reference proteome {ECO:0000313|Proteomes:UP000002438}. FT DOMAIN 93..148 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 152..210 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT ACT_SITE 304 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT ACT_SITE 402 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT BINDING 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AHN" FT BINDING 98 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 120 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 135 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:7QDX" FT BINDING 136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 137 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 153 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 159 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 178 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW" FT BINDING 180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:7QDX" FT BINDING 180 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:7QDX" FT BINDING 180 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:4DQW" FT BINDING 181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4DQW, ECO:0007829|PDB:7QDX" FT BINDING 247..249 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3" FT BINDING 247 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 297..299 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-3" FT BINDING 299 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT BINDING 301 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT BINDING 302 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 302 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AHN" FT BINDING 302 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 304 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT BINDING 337..339 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 337 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 337 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AHN" FT BINDING 339 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 339 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AHN" FT BINDING 360..361 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 360 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 360 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AHN" FT BINDING 361 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 361 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AHN" FT BINDING 384..388 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 384 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 387 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 388 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AHM" FT BINDING 417 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 471 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 472 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 473 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" SQ SEQUENCE 489 AA; 51707 MW; 6D2320AFD52C888B CRC64; MLRISQEALT FDDVLLIPGY SEVLPKDVSL KTRLTRGIEL NIPLVSAAMD TVTEARLAIA MAQEGGIGII HKNMGIEQQA AEVRKVKKHE TAIVRDPVTV TPSTKIIELL QMAREYGFSG FPVVEQGELV GIVTGRDLRV KPNAGDTVAA IMTPKDKLVT AREGTPLEEM KAKLYENRIE KMLVVDENFY LRGLVTFRDI EKAKTYPLAS KDEQGRLRVG AAVGTGADTG ERVAALVAAG VDVVVVDTAH GHSKGVIERV RWVKQTFPDV QVIGGNIATA EAAKALAEAG ADAVKVGIGP GSICTTRIVA GVGVPQISAI ANVAAALEGT GVPLIADGGI RFSGDLAKAM VAGAYCVMMG SMFAGTEEAP GEIELFQGRS YKSYRGMGSL GAMSGSQGSS DRYFQDASAG AEKLVPEGIE GRVPYKGALS AIVHQLMGGL RAAMGYTGSA DIQQMRTQPQ FVRITGAGMA ESHVHDVQIT KEAPNYRVG //