ID D8VEH1_CHLPN Unreviewed; 214 AA.
AC D8VEH1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=IMP dehydrogenase {ECO:0000313|EMBL:ADI88856.1};
DE Flags: Fragment;
GN Name=guaB {ECO:0000313|EMBL:ADI88856.1};
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558 {ECO:0000313|EMBL:ADI88856.1};
RN [1] {ECO:0000313|EMBL:ADI88856.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DE177 {ECO:0000313|EMBL:ADI88856.1};
RX PubMed=20502684; DOI=10.1371/journal.ppat.1000903;
RA Mitchell C.M., Hutton S., Myers G.S.A., Brunham R., Timms P.;
RT "Chlamydia pneumoniae is genetically diverse in animals and appears to have
RT crossed the host barrier to humans on (at least) two occasions.";
RL PLoS Pathog. 6:E1000903-E1000903(2010).
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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502}.
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DR EMBL; GQ918211; ADI88856.1; -; Genomic_DNA.
DR AlphaFoldDB; D8VEH1; -.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00478; IMPDH; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 1..214
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADI88856.1"
FT NON_TER 214
FT /evidence="ECO:0000313|EMBL:ADI88856.1"
SQ SEQUENCE 214 AA; 22198 MW; 77C47F555637CA0F CRC64;
DTAHAHSKGV FQTVLEIKSQ FPQISLVVGN LVIAEAAVSL AEIGVDAVKV GIGPGSICTT
RIVSGVGYPQ ITAITNVAKA LKNSAVTVIA DGGIRYSGDV VKALAAGADC VMLGSLLAGT
DEAPGDIVSI DEKLFKRYRG MGSLGAMKQG SADRYFQTQG QKKLVPEGVE GLVAYKGSVH
DVLYQILGGI RSGMGYVGAE TLKDLKTKAS FVRI
//
