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Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)

 A0A0R1PVZ2_9LACO        Unreviewed;       492 AA.
A0A0R1PVZ2;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
27-SEP-2017, entry version 13.
RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964};
Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964};
Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964};
EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964};
ORFNames=FD33_GL000572 {ECO:0000313|EMBL:KRL32408.1};
Lactobacillus paralimentarius DSM 13238 = JCM 10415.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
Lactobacillus.
NCBI_TaxID=1122151 {ECO:0000313|EMBL:KRL32408.1, ECO:0000313|Proteomes:UP000051908};
[1] {ECO:0000313|EMBL:KRL32408.1, ECO:0000313|Proteomes:UP000051908}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 13238 {ECO:0000313|EMBL:KRL32408.1,
ECO:0000313|Proteomes:UP000051908};
PubMed=26415554; DOI=10.1038/ncomms9322;
Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
"Expanding the biotechnology potential of lactobacilli through
comparative genomics of 213 strains and associated genera.";
Nat. Commun. 6:8322-8322(2015).
-!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP)
to xanthosine 5'-phosphate (XMP), the first committed and rate-
limiting step in the de novo synthesis of guanine nucleotides, and
therefore plays an important role in the regulation of cell
growth. {ECO:0000256|HAMAP-Rule:MF_01964}.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01964};
-!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive
inhibitor that prevents formation of the closed enzyme
conformation by binding to the same site as the amobile flap. In
contrast, mizoribine monophosphate (MZP) is a competitive
inhibitor that induces the closed conformation. MPA is a potent
inhibitor of mammalian IMPDHs but a poor inhibitor of the
bacterial enzymes. MZP is a more potent inhibitor of bacterial
IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}.
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP-
Rule:MF_01964, ECO:0000256|RuleBase:RU003927}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KRL32408.1}.
-----------------------------------------------------------------------
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EMBL; AZES01000012; KRL32408.1; -; Genomic_DNA.
RefSeq; WP_025084825.1; NZ_BAMH01000010.1.
EnsemblBacteria; KRL32408; KRL32408; FD33_GL000572.
PATRIC; fig|1122151.5.peg.596; -.
UniPathway; UPA00601; UER00295.
Proteomes; UP000051908; Unassembled WGS sequence.
GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00381; IMPDH; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005990; IMP_DH.
InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
InterPro; IPR001093; IMP_DH_GMPRt.
Pfam; PF00571; CBS; 2.
Pfam; PF00478; IMPDH; 1.
PIRSF; PIRSF000130; IMPDH; 1.
SMART; SM00116; CBS; 2.
TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS00487; IMP_DH_GMP_RED; 1.
3: Inferred from homology;
CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
Complete proteome {ECO:0000313|Proteomes:UP000051908};
GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928};
NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3,
ECO:0000256|RuleBase:RU003928};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003927};
Potassium {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|RuleBase:RU003928}.
DOMAIN 97 155 CBS. {ECO:0000259|PROSITE:PS51371}.
DOMAIN 159 216 CBS. {ECO:0000259|PROSITE:PS51371}.
NP_BIND 253 255 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.
NP_BIND 303 305 NAD. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-3}.
REGION 343 345 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
REGION 366 367 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
REGION 390 394 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
ACT_SITE 310 310 Thioimidate intermediate.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-1}.
ACT_SITE 406 406 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-1}.
METAL 305 305 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 307 307 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 310 310 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 474 474 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_01964}.
METAL 475 475 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_01964}.
METAL 476 476 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_01964}.
BINDING 253 253 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.
BINDING 308 308 IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
BINDING 421 421 IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
ECO:0000256|PIRSR:PIRSR000130-2}.
SEQUENCE 492 AA; 52337 MW; 9A8C577E659E307F CRC64;
MSAWDTKFDK KGFTFDDVLL IPAESHVLPN EVDLSVQLAK NIKLNTPILS ASMDTVTEAP
MAIAMARQGG LGVIHKNMSI EQQADEVSKV KRSENGVIID PIYLTADDKV SEAEKLMSTY
RISGVPIVTN TTDLKLVGII TNRDLRFITD FSVKIGTVMT SEELITAPVG TSLKEAEQIL
QEHKIEKLPL IDKNGRLGGL VTIKDIEKVK EFPNAAKDQY GRLLVAAAVG VTSDTFERAE
ALLDAGADAI IIDTAHGHSA GVLRKISEIR NKFPEATLIA GNVATAEGTR ALYDAGVDVV
KVGIGPGSIC TTRIVAGVGV PQLTAVYDAA SVAHEYGKTI IADGGIKYSG DIVKALAGGG
NAVMLGSMLA GTDEAPGEFE IYQGRRFKTY RGMGSLAAMS HGSSDRYFQS GVNEANKLVP
EGIEGRVAAK GAVGDVIYQL LGGLRSGMGY VGAHNLKELQ DAQFVQISNA GLRESHPHDV
TITKEAPNYS VK


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