ID W4BP61_9BACL Unreviewed; 504 AA.
AC W4BP61;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Inosine 5-monophosphate dehydrogenase {ECO:0000313|EMBL:ETT45127.1};
DE EC=1.1.1.205 {ECO:0000313|EMBL:ETT45127.1};
GN ORFNames=C162_21358 {ECO:0000313|EMBL:ETT45127.1};
OS Paenibacillus sp. FSL R7-269.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1226755 {ECO:0000313|EMBL:ETT45127.1, ECO:0000313|Proteomes:UP000019056};
RN [1] {ECO:0000313|EMBL:ETT45127.1, ECO:0000313|Proteomes:UP000019056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-269 {ECO:0000313|EMBL:ETT45127.1,
RC ECO:0000313|Proteomes:UP000019056};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT45127.1}.
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DR EMBL; ASPS01000049; ETT45127.1; -; Genomic_DNA.
DR RefSeq; WP_036697488.1; NZ_ASPS01000049.1.
DR AlphaFoldDB; W4BP61; -.
DR PATRIC; fig|1226755.4.peg.4258; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000019056; 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; 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:ETT45127.1};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 103..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 504 AA; 55654 MW; FD5E6161AB25912D CRC64;
MAYYYEQPSR TFSEFLLVPS LTTKDCIPGN VDLSTPVTKF RRGETPALTM NLPVTSAVMQ
AVSDHNMAIA LAKSGGISFI YGSQSITQQV EMVRRVKKFK AGFVLSDSNL RPEDTLQDVL
VLKARSGHST IAITDNGEPT GRLMGIVTSR DYRENRLPPD CPITEFMTPL ASLIYAEEGI
TLTEANDMIW DHKLNCLPIV NDSGHLVHLV FRKDYDSHQE YPLELHDDNK QLIVGAGINS
RDYKERVPAL VEAGADILCI DSSDGYSEWQ AETIHYIKET FGESVKVGAG NVVDKEGFLY
LVEAGADFIK VGIGGGSICI TREQKGIGRG QASSVIEVAA ARQEYYEQTG IYVPICSDGG
IVYDYHIVLA LAMGADFVML GRYFARFDES PGRKLLVGGN FVKEYWGEGS SRARNWQRYD
FGNADKESKL EFEEGVDSFI PYAGRLKDNL DLSISKIKST MCNCGALTIP ELQQKAKITL
VSSTTIFEGG AHDVMLKEKD RSSS
//
