ID A0A0G1FBA7_9BACT Unreviewed; 365 AA.
AC A0A0G1FBA7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=IMP dehydrogenase (Inosine-5'-monophosphate dehydrogenase) {ECO:0000313|EMBL:KKS84103.1};
GN ORFNames=UV59_C0027G0031 {ECO:0000313|EMBL:KKS84103.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA1_43_11.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618436 {ECO:0000313|EMBL:KKS84103.1, ECO:0000313|Proteomes:UP000034543};
RN [1] {ECO:0000313|EMBL:KKS84103.1, ECO:0000313|Proteomes:UP000034543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
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:KKS84103.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCFB01000027; KKS84103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FBA7; -.
DR STRING; 1618436.UV59_C0027G0031; -.
DR PATRIC; fig|1618436.3.peg.1195; -.
DR Proteomes; UP000034543; Unassembled WGS sequence.
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; 2.
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 14..353
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
SQ SEQUENCE 365 AA; 38767 MW; 21DA2D9F64FE8090 CRC64;
MNNTNPLLNI PEYLTYDDVL LLPNYSEVRP SQTQVQTQLT DQIRLDIPIV ASPMDTVCEA
EMAIALGELG GLGIIHRNLS IADQVQQVER VLKAKITVAA AVGVGSDFNE RTEALVKTGI
KILCIDSAHG HTKHVIEATK LIKIKYPKIE LLSGNVATYE GAKALFAAGA DAVKVGMGPG
SICTTRVMSG MGVPQLTAVV EGVRAAREFK KYVIADGGIR TSGDIVKALA AGASTVMLGS
LLAGTDEAPG EVVQMGDKLY KTYRGMGSVA AMKHGSATRY GQKWEKGKTK ELVPEGVEGL
VAHKGPLADH IHQLIGGARA GMGYLGAKTI SELHQKAKFI KITNASLIES HPHNLVITNP
GKNYV
//
