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Database: UniProt
Entry: A0A0Q6MLL0_9BURK
LinkDB: A0A0Q6MLL0_9BURK
Original site: A0A0Q6MLL0_9BURK 
ID   A0A0Q6MLL0_9BURK        Unreviewed;       489 AA.
AC   A0A0Q6MLL0;
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=ASC88_16230 {ECO:0000313|EMBL:KQU81069.1};
OS   Rhizobacter sp. Root29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU81069.1, ECO:0000313|Proteomes:UP000051195};
RN   [1] {ECO:0000313|EMBL:KQU81069.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU81069.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU81069.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU81069.1,
RC   ECO:0000313|Proteomes:UP000051195};
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:KQU81069.1}.
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DR   EMBL; LMCN01000003; KQU81069.1; -; Genomic_DNA.
DR   RefSeq; WP_056814637.1; NZ_LMCN01000003.1.
DR   AlphaFoldDB; A0A0Q6MLL0; -.
DR   STRING; 1736511.ASC88_16230; -.
DR   OrthoDB; 9805398at2; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000051195; 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:UP000051195}.
FT   DOMAIN          92..147
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          151..212
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        303
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        399
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         246..248
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         296..298
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         298
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         300
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="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         303
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         336..338
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         359..360
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         383..387
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         417
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
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;  51967 MW;  6B174290D0DE27A3 CRC64;
     MRLLGKALTF DDVLLVPAFS QVLPRDTSLA TQLSRNIRLN LPLVSAAMDT VTEARLAIAI
     AQEGGIGIVH KNLSPKQQAA EVARVKRYES GVLRDPITIS PGVPVRDVIN LSRQHGISGF
     PVLEDGKVVG IVTGRDLRFE TRMDIPVREI MTPRERLITV RDGASLADAK ALMHKHKLER
     VVVVNDAFEL RGLFTVKDIT KQTNFPNAAR DSHGKLRVGA AVGVGEDTDE RLELLVKAGV
     DAVVVDTAHG HSAGVLDRVR WVKKNYPQID VIGGNIATGA AALALVEAGA DGVKVGIGPG
     SICTTRIVAG VGVPQITAID NVATALKGTG VPLIADGGVR YSGDIAKAIA AGACTVMMGG
     MFAGTEEAPG EIVLFQGRSY KSYRGMGSIG AMQQGSADRY FQDNTGANPN ADKLVPEGIE
     GRVPYKGSMV SIVFQMAGGL RASMGYCGCP TIDDMRDRAE FVEITSAGIR ESHVHDVQIT
     KEAPNYRME
//
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