ID Q9KTW3_VIBCH Unreviewed; 489 AA. AC Q9KTW3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 149. 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 OrderedLocusNames=VC_0767 {ECO:0000313|EMBL:AAF93932.1}; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93932.1, ECO:0000313|Proteomes:UP000000584}; RN [1] {ECO:0000313|EMBL:AAF93932.1, ECO:0000313|Proteomes:UP000000584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961 RC {ECO:0000313|Proteomes:UP000000584}; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D., RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L., RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). RN [2] {ECO:0007829|PDB:4FEZ} RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 1-92 AND 200-489. RA Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., RA Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion RT mutant."; RL Submitted (MAY-2012) to the PDB data bank. RN [3] {ECO:0007829|PDB:4FO4} RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-90 AND 220-489. RA Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., RA Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion RT mutant, complexed with IMP and mycophenolic acid."; RL Submitted (JUN-2012) to the PDB data bank. RN [4] {ECO:0007829|PDB:4FXS} RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH IMP. RA Osipiuk J., Maltseva N., Makowska-Grzyska M., Jedrzejczak R., RA Anderson W.F., Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae complexed with RT IMP and mycophenolic acid."; RL Submitted (JUL-2012) to the PDB data bank. RN [5] {ECO:0007829|PDB:4IX2} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH RP IMP. RA Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., RA Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion RT mutant, complexed with IMP."; RL Submitted (JAN-2013) to the PDB data bank. RN [6] {ECO:0007829|PDB:4QNE} RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH RP NAD. RA Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., RA Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion RT mutant, in complex with NAD and IMP."; RL Submitted (JUN-2014) to the PDB data bank. RN [7] {ECO:0007829|PDB:4QQ3} RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH RP XMP. RA Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., RA Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from vibrio cholerae, deletion RT mutant, in complex with xmp."; RL Submitted (JUN-2014) to the PDB data bank. RN [8] {ECO:0007829|PDB:4X3Z} RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH RP NAD(+) AND XMP. RG Center for Structural Genomics of Infectious Diseases (CSGID); RA Osipiuk J., MALTSEVA N., KIM Y., Mulligan R., MAKOWSKA-GRZYSKA M., Gu M., RA Anderson W.F., Joachimiak A.; RT "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion RT mutant, in complex with XMP and NAD."; RL Submitted (DEC-2014) to the PDB data bank. 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 -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_01964, CC ECO:0000256|RuleBase:RU003927}. 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; AE003852; AAF93932.1; -; Genomic_DNA. DR PIR; C82282; C82282. DR RefSeq; NP_230416.1; NC_002505.1. DR PDB; 4FEZ; X-ray; 2.16 A; A/B=1-489. DR PDB; 4FO4; X-ray; 2.03 A; A/B=1-489. DR PDB; 4FXS; X-ray; 2.24 A; A=1-489. DR PDB; 4IX2; X-ray; 2.15 A; A/B/C/D=1-90, A/B/C/D=220-489. DR PDB; 4QNE; X-ray; 2.32 A; A/B=1-90, A/B=220-489. DR PDB; 4QQ3; X-ray; 1.72 A; A=1-90, A=220-489. DR PDB; 4X3Z; X-ray; 1.62 A; A/B=1-90, A/B=220-489. DR PDBsum; 4FEZ; -. DR PDBsum; 4FO4; -. DR PDBsum; 4FXS; -. DR PDBsum; 4IX2; -. DR PDBsum; 4QNE; -. DR PDBsum; 4QQ3; -. DR PDBsum; 4X3Z; -. DR AlphaFoldDB; Q9KTW3; -. DR SMR; Q9KTW3; -. DR STRING; 243277.VC_0767; -. DR DNASU; 2615310; -. DR EnsemblBacteria; AAF93932; AAF93932; VC_0767. DR KEGG; vch:VC_0767; -. DR PATRIC; fig|243277.26.peg.731; -. DR eggNOG; COG0516; Bacteria. DR eggNOG; COG0517; Bacteria. DR HOGENOM; CLU_022552_2_2_6; -. DR BRENDA; 1.1.1.205; 6626. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000584; Chromosome 1. 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:0000166; F:nucleotide 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:4FEZ, ECO:0007829|PDB:4FO4}; 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:4QNE, ECO:0007829|PDB:4X3Z}; 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:UP000000584}. FT DOMAIN 95..154 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 155..216 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT ACT_SITE 307 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT ACT_SITE 403 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT BINDING 250..252 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 250 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" FT BINDING 250 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" FT BINDING 252 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 252 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" FT BINDING 253 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 256 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 300..302 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 300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" FT BINDING 300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 302 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 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 305 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 305 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 305 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 307 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" FT BINDING 307 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 307 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 308 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 309 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 309 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 340..342 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 340 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 340 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 340 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 342 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 342 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 342 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 363..364 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 363 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 363 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 363 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 364 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 364 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 364 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 387..391 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 387 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 387 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 387 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 390 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 390 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 390 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4QQ3" FT BINDING 391 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0007829|PDB:4FO4, ECO:0007829|PDB:4FXS" FT BINDING 391 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" 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 417 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4X3Z" FT BINDING 442 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4QNE" 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; 51943 MW; B38133B52F8661C4 CRC64; MHMLRIAKEA LTFDDVLLVP AHSTVLPNTA DLRTRLTKNI ALNIPMVSAS MDTVTEARLA IALAQEGGIG FIHKNMSIEQ QAAQVHQVKI FEAGVVTHPV TVRPEQTIAD VMELTHYHGF AGFPVVTENN ELVGIITGRD VRFVTDLTKS VAAVMTPKER LATVKEGATG AEVQEKMHKA RVEKILVVND EFQLKGMITA KDFHKAESKP NACKDEQGRL RVGAAVGAAP GNEERVKALV EAGVDVLLID SSHGHSEGVL QRIRETRAAY PHLEIIGGNV ATAEGARALI EAGVSAVKVG IGPGSICTTR IVTGVGVPQI TAIADAAGVA NEYGIPVIAD GGIRFSGDIS KAIAAGASCV MVGSMFAGTE EAPGEVILYQ GRSYKAYRGM GSLGAMSKGS SDRYFQTDNA ADKLVPEGIE GRIAYKGHLK EIIHQQMGGL RSCMGLTGSA TVEDLRTKAQ FVRISGAGMK ESHVHDVQIT KEAPNYRLG //