ID A0A3M8AJ60_9BACL Unreviewed; 499 AA.
AC A0A3M8AJ60;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=IMP dehydrogenase {ECO:0000313|EMBL:RNB51218.1};
DE EC=1.1.1.205 {ECO:0000313|EMBL:RNB51218.1};
GN ORFNames=EDM57_22455 {ECO:0000313|EMBL:RNB51218.1};
OS Brevibacillus gelatini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1655277 {ECO:0000313|EMBL:RNB51218.1, ECO:0000313|Proteomes:UP000268829};
RN [1] {ECO:0000313|EMBL:RNB51218.1, ECO:0000313|Proteomes:UP000268829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100115 {ECO:0000313|EMBL:RNB51218.1,
RC ECO:0000313|Proteomes:UP000268829};
RA Dunlap C.;
RT "Phylogenomics of Brevibacillus.";
RL Submitted (OCT-2018) 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:RNB51218.1}.
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DR EMBL; RHHS01000070; RNB51218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8AJ60; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000268829; 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; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 1.
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:RNB51218.1};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 167..225
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 317
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 261..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 310..312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 312
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 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 317
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 499 AA; 54788 MW; 8F90774E946AED24 CRC64;
MAIYYTEPSR TFNEFLLLPN LTTKECTPNN VDLSTPITKF KKGEKPAIKL NIPFSSAVMQ
AVSDHHMAVA LARCGGISFI FGSQSIESQA NMVRKVKNHK AGFVVSRSNL TPSHTLKDIL
ELKEQTGHST VAVTEDGSAK GKLLGIVTGR DYRISRDSLD KPVSEIMTPF SSLIYGKSGI
TLSEANDLIW EHKLNCLPIV DDNQHLDFLV FRKDYDSRKN NPLSLLDANK SYIVGAGINT
KDYQERVPAL VEAGVDVLVI DSSDGFSEWQ RDTVQYVKQN FNVPIGAGNV VDKEGFRYLV
EAGADFVKVG IGGGSICITR EQKGIGRGQA SAVIEVAAAR DEYFKETGIY VPICSDGGIV
HDYHVTLALA MGADFVMLGR YFARFDESPT KKVKIGNNFV KEYWGEGSNR ARNWQRYDTG
GKSSLVFEEG VDSYVPYAGS LRENLDRTLS KIKSTMCNCG SLSISELQQK ARITLISATS
LIEGGAHDVI LKESTMAAE
//
