ID A0A0Q6PS53_9MICO Unreviewed; 500 AA.
AC A0A0Q6PS53;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=ASC63_07860 {ECO:0000313|EMBL:KQV07221.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV07221.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV07221.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV07221.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV07221.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV07221.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQV07221.1}.
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DR EMBL; LMCU01000001; KQV07221.1; -; Genomic_DNA.
DR RefSeq; WP_055811627.1; NZ_LMCU01000001.1.
DR AlphaFoldDB; A0A0Q6PS53; -.
DR STRING; 1736426.ASC63_07860; -.
DR OrthoDB; 9805398at2; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000051914; 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:UP000051914}.
FT DOMAIN 96..152
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 159..216
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 312
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 253..255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT BINDING 305..307
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 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 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 310
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 312
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 345..347
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 368..369
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 392..396
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 429
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 483
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 484
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 485
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 500 AA; 52818 MW; 97C1EA6E60937EC3 CRC64;
MDQSDPFGFI GLTYDDVMLL PGHTDVIPSE ADTSTRLTKR ITVASPLLSS AMDTVTEARM
AIAMARNGGI GILHRNLSIE DQAAFVDKVK RSESGMITNP VTTTPDATVA EVDALCGQFR
VSGLPVVEAD GTLVGIITNR DMRFVSVSEK STTLVRDVMT HAPLITAAVG IDPETAVSIF
AEHKIEKLPL VDADGKLTGL ITVKDFDKSE QYPNATKDDE GRLRVGAAIG FFGDAWERAM
ALVDAGVDVL VVDTANGDSA GVIDIIRRLK AEPRAAHVDI IGGNVATRAG AQALIDAGVD
AVKVGVGPGS ICTTRVVAGV GVPQVTAVYE ASLAAREAGV PVIADGGLQY SGDIAKALVA
GADSVMLGSL LAGCDESPGD LVFVNGKQFK NYRGMGSLGA LQTRGKKTSY SRDRYFQADV
PSDEQLIAEG IEGQVPYRGP LSAVSYQLIG GLRQSMFYVG ARTISELKER GKFVRITAAG
LKESHPHDIQ MVVEAPNYRR
//
