ID A8REZ0_9FIRM Unreviewed; 503 AA.
AC A8REZ0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Inosine 5-monophosphate dehydrogenase {ECO:0000313|EMBL:EDP10096.1};
DE EC=1.1.1.205 {ECO:0000313|EMBL:EDP10096.1};
GN ORFNames=EUBDOL_02110 {ECO:0000313|EMBL:EDP10096.1};
OS Amedibacillus dolichus DSM 3991.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Amedibacillus.
OX NCBI_TaxID=428127 {ECO:0000313|EMBL:EDP10096.1, ECO:0000313|Proteomes:UP000004090};
RN [1] {ECO:0000313|EMBL:EDP10096.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10096.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium dolichum (DSM 3991).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDP10096.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10096.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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:EDP10096.1}.
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DR EMBL; ABAW02000025; EDP10096.1; -; Genomic_DNA.
DR RefSeq; WP_004800749.1; NZ_DS483478.1.
DR AlphaFoldDB; A8REZ0; -.
DR STRING; 428127.EUBDOL_02110; -.
DR GeneID; 83059498; -.
DR eggNOG; COG0516; Bacteria.
DR eggNOG; COG0517; Bacteria.
DR HOGENOM; CLU_022552_2_1_9; -.
DR Proteomes; UP000004090; Unassembled WGS sequence.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04601; CBS_pair_IMPDH; 1.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00571; CBS; 1.
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}; GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000130-3};
KW Oxidoreductase {ECO:0000313|EMBL:EDP10096.1};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 98..163
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 167..225
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 261..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 312..314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 314
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|PIRSR:PIRSR000130-4"
FT BINDING 316
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|PIRSR:PIRSR000130-4"
FT BINDING 319
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|PIRSR:PIRSR000130-4"
SQ SEQUENCE 503 AA; 55384 MW; F59CB8432FBA0B83 CRC64;
MAYFFDEPSR TFSEYLLVPG YSSAECTPAN VSLKTPLVKF RKGEKSAIEL NIPMVSAIMQ
SVSGERMACA LAREGGISFI YGSQSVEDEA AMVRRVKATK AGFVYSDSNI RPDATLQEVL
ALKERNGHAT MAVTEDGTAN GKLVGIITSR DYRVTRMDLN TKVEDFMTPF DKLICAKEGC
SLSEANDIIW EHKLNQLPII DDQQNLVAFV FRKDYDSHKE NPNEVLDAKK RYLVGAGVNT
RDYETRIPAL VEAGADVLCI DSSEGFSEWQ ARTLAWVRER YGDSVKIGAG NVVDAEGFRF
LAEAGADFIK IGIGGGSICI TREQKGIGRG QATATIEVAK ARDEYYKETG IYIPICSDGG
IVHDYHITLA LAMGADFVML GRYFSRFEES PTKKVTVNGT YMKEYWGEGS ARARNWQRYD
MGGNQKLSFV EGVDSYVPYA GALKDNVDLT LSKVKHTMCN CGALTIPELQ EKAKITLVSS
TSIVEGGAHD VVVKDNTYDA KVK
//
