ID N2BJ58_9ACTN Unreviewed; 505 AA.
AC N2BJ58;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000313|EMBL:EMZ41807.1};
GN ORFNames=HMPREF1091_00781 {ECO:0000313|EMBL:EMZ41807.1};
OS Atopobium minutum 10063974.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=997872 {ECO:0000313|EMBL:EMZ41807.1, ECO:0000313|Proteomes:UP000012651};
RN [1] {ECO:0000313|EMBL:EMZ41807.1, ECO:0000313|Proteomes:UP000012651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10063974 {ECO:0000313|EMBL:EMZ41807.1,
RC ECO:0000313|Proteomes:UP000012651};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Lambert T., Marvaud J.-C.,
RA Courvalin P., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Atopobium minutum 10063974.";
RL Submitted (MAR-2013) 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:EMZ41807.1}.
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DR EMBL; AGXC01000002; EMZ41807.1; -; Genomic_DNA.
DR RefSeq; WP_002563556.1; NZ_KB822533.1.
DR AlphaFoldDB; N2BJ58; -.
DR PATRIC; fig|997872.3.peg.783; -.
DR HOGENOM; CLU_022552_2_1_11; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000012651; 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; 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; 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 Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000012651}.
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 505 AA; 55477 MW; 79AD0EA360F2B9DE CRC64;
MATFFEGESH TFSEYLLVPG YSSSQNVPAN VSLKTPLVKF KRGEQSAITM NIPMVSAIMQ
AVSGPRLAIA LAQQGGISFI YGSQTPEDEA SMVREVKSYK AGFVISDSTL TPAMTLQDVL
DIRDTTGHTT MPVTEDGQPF GKFCGIVTSR DYRVSRDDRN LKVSEFMTPA SECVTADPSV
SLKECNDIIW DNKVNTLPIV DKNGNLCSLV FRKDYDSHKA RPEELLDEHK RYIVGAGINT
RDYAERVPLL VEAGADVLCI DSSEGFSEWQ KLTLDWIREH YGDRVKVGAG NVVDAEGFRY
LAQCGADFVK VGIGGGSICI TREQKGIGRG QASALIDVCR ARDEYYEETG VYVPVCSDGG
IVYDYHMTLA LAMGADFLML GRYFARFDES PTRRVNVNGS YMKEYWGEGS ARARNWARYD
LGGSKKQLSF VEGVDSYVPY AGPLKDNVDG SLTKVRSTMC NCGALDLAEL REKAKITLVS
ATSLVEGGAH DVMLKDSPAE NNFRS
//
