ID A0A1G9ZCM6_9BACI Unreviewed; 488 AA.
AC A0A1G9ZCM6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=SAMN05216498_1632 {ECO:0000313|EMBL:SDN18847.1};
OS Tenuibacillus multivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tenuibacillus.
OX NCBI_TaxID=237069 {ECO:0000313|EMBL:SDN18847.1, ECO:0000313|Proteomes:UP000199334};
RN [1] {ECO:0000313|EMBL:SDN18847.1, ECO:0000313|Proteomes:UP000199334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3442 {ECO:0000313|EMBL:SDN18847.1,
RC ECO:0000313|Proteomes:UP000199334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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,
CC ECO:0000256|HAMAP-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}.
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DR EMBL; FNIG01000003; SDN18847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ZCM6; -.
DR STRING; 237069.SAMN05216498_1632; -.
DR OrthoDB; 9805398at2; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000199334; Unassembled WGS sequence.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
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 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 3: Inferred from homology;
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 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:UP000199334}.
FT DOMAIN 96..156
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 158..216
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 309
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 405
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 252..254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT BINDING 302..304
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 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 306
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 307
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 309
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 342..344
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 365..366
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 389..393
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="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 488 AA; 52892 MW; FC6B1C9313E9C6F9 CRC64;
MVWEQKFQKE GLTFDDVLLM PAQSDVLPRE VDIQVALTDS LKLKTPIISA GMDTVTEADM
AIAMARQGGL GVIHKNMSIE EQADQVDKVK RSIRGVITNP FFLTPEHQVF DAEHLMGKYR
ISGVPIVNNE VDQELIGIIT NRDLRFIEEY SSRISEVMTK KDLVTAPVNT SLEEAERILQ
QHKIEKLPLV DDDNRLKGLI TIKDIEKVIE FPNTAVDAKG RLLVAAAIGV TADVMLRAEK
LIDAGVDALV VDTAHGHSQG VLDTIKRLKE AYPSVDLIAG NVATPKATRA LIDAGADVIK
VGIGPGSICT TRVVAGVGVP QISAVYDCAT EARKHGVAII ADGGIKFSGD IVKALAAGGH
AVMLGSMFAG TSESPGETEI FQGRRYKVYR GMGSVGAMEK GSKDRYFQED NKKFVPEGIE
GRVPYKGPLA ETIYQLTGGL RSGMGYCGAE NLEKLREDAQ FVKITNAGLK ESHPHDIQVT
KEAPNYSL
//
