IMDH_KORCO
ID IMDH_KORCO Reviewed; 476 AA.
AC B1L5U5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000250|UniProtKB:P0ADG7};
DE Short=IMP dehydrogenase {ECO:0000250|UniProtKB:P0ADG7};
DE Short=IMPD {ECO:0000250|UniProtKB:P0ADG7};
DE Short=IMPDH {ECO:0000250|UniProtKB:P0ADG7};
DE EC=1.1.1.205 {ECO:0000250|UniProtKB:P0ADG7};
GN Name=guaB {ECO:0000250|UniProtKB:P0ADG7}; OrderedLocusNames=Kcr_1078;
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX NCBI_TaxID=374847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8;
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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:0000250|UniProtKB:P0ADG7}.
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:0000250|UniProtKB:P0ADG7};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P0ADG7};
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:0000250|UniProtKB:P0ADG7}.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC from IMP: step 1/1. {ECO:0000250|UniProtKB:P0ADG7}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0ADG7}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000305}.
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DR EMBL; CP000968; ACB07824.1; -; Genomic_DNA.
DR RefSeq; WP_012309721.1; NC_010482.1.
DR AlphaFoldDB; B1L5U5; -.
DR SMR; B1L5U5; -.
DR STRING; 374847.Kcr_1078; -.
DR EnsemblBacteria; ACB07824; ACB07824; Kcr_1078.
DR GeneID; 6094355; -.
DR KEGG; kcr:Kcr_1078; -.
DR eggNOG; arCOG00612; Archaea.
DR HOGENOM; CLU_022552_2_1_2; -.
DR InParanoid; B1L5U5; -.
DR OMA; MGYCGAK; -.
DR OrthoDB; 58700at2157; -.
DR PhylomeDB; B1L5U5; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000001686; Chromosome.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR11911; PTHR11911; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW CBS domain; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase;
KW Potassium; Purine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..476
FT /note="Inosine-5'-monophosphate dehydrogenase"
FT /id="PRO_0000415693"
FT DOMAIN 93..151
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 152..211
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT ACT_SITE 299
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKI7"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT BINDING 292..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT BINDING 294
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:0000250|UniProtKB:P50097"
FT BINDING 296
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:0000250|UniProtKB:P50097"
FT BINDING 297
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P50097"
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:0000250|UniProtKB:P50097"
FT BINDING 334..336
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT BINDING 357..358
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT BINDING 381..385
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT BINDING 408
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P50097"
FT BINDING 462
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000250|UniProtKB:P50097"
SQ SEQUENCE 476 AA; 51195 MW; 6AAC31F930E62260 CRC64;
MRIDRFEFAF TFNDVILLPG KTEIEPSNVD LTTRIGNIAL SIPILSSPMD TVTEEEMSIA
MARMGGLGIL HRNCSVEEQV NMAKAVKRAE SFIIRDVITV SPEDSVEEAR RLMREHGISG
LPVIVGRKLV GIVTRRDVYF AENGSLLVKD IMTKDPITVG PEITPQEARK IMARYKIEKL
PVVSESGELI GLVTAKDVFY RESHPFATRD EEGRLRVGAA ISPFDIDRAK TLAPYVDVLV
TDVAHFHNEN VISATKRIID EVGVPVIAGN IGTYEAAEEA ITRLDIIGLR VGIGSGSICT
TGEVTGVAAP TLYAVASASE AVRKYSKDVA VIADGGIRGP GEAAKAFAMG ADAVMLGYAL
AGTKEAPGST MMIGGKMYKI YRGMGSPSAR SKRFAMDRYS KPSKDIAEGI EGLVPYRGDV
TTVVDRFVAG LKAAFGYVGA ANISEMKSKA RVALISHSGM SEIAPHDVKP LEKISD
