ID S3A7H5_9ACTN Unreviewed; 507 AA.
AC S3A7H5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000313|EMBL:EPD78167.1};
GN ORFNames=HMPREF1527_00475 {ECO:0000313|EMBL:EPD78167.1};
OS Atopobium sp. oral taxon 199 str. F0494.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=1203602 {ECO:0000313|EMBL:EPD78167.1, ECO:0000313|Proteomes:UP000014384};
RN [1] {ECO:0000313|EMBL:EPD78167.1, ECO:0000313|Proteomes:UP000014384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0494 {ECO:0000313|EMBL:EPD78167.1,
RC ECO:0000313|Proteomes:UP000014384};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Tanner A.C.,
RA Dewhirst F.D., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Atopobium sp. oral taxon 199 F0494.";
RL Submitted (MAY-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:EPD78167.1}.
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; ATCH01000001; EPD78167.1; -; Genomic_DNA.
DR RefSeq; WP_016477104.1; NZ_KE150486.1.
DR AlphaFoldDB; S3A7H5; -.
DR STRING; 1203602.HMPREF1527_00475; -.
DR PATRIC; fig|1203602.3.peg.478; -.
DR eggNOG; COG0516; Bacteria.
DR eggNOG; COG0517; Bacteria.
DR HOGENOM; CLU_022552_2_1_11; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000014384; 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; 2.
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 Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000014384}.
FT DOMAIN 103..165
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 507 AA; 55321 MW; DCA7401E88AC8FEC CRC64;
MAKFFEGESH TFSEYLLVPG YSSAENIPAN VSLKTPLVKF KRGEEPSLSL NIPMVSAVMQ
AVSGPRLAIA LAQQGGLSFI YGSQSAEDEA QMVREVKSYK AGFVVSDSTL TPDMTLAEVL
DLKEKTGHST MPVTTDGTSY GKLVGIVTSR DYRPSRDEVT KKVAEFMTPV DAIISAPETT
TLKEANDIIW DNKLNALPIV DTNGYLVSLV FRKDYDSHKS APNELLDASK RYLVGAGINT
RDYETRVPLL VEAGADVLCI DSSEGYSEWQ ARTLKWIRQT YGDGVKVGAG NVVDAEGFRF
LADAGADFIK IGIGGGSICI TREQKGIGRG QATSVIDVAR ARDAYFEETG VYIPICSDGG
IVYDYHMTLA LAMGSDFMML GRYFARFDES PSNRVNVNGS YMKEYWGEGS ARARNWQRYD
LGGNKRGLSF VEGVDSYVPY AGSLKDGVEG SLLKVKSTMC NCGARDIVEL REKAKITLVS
ATSIVEGGAH DVLLKDQNQQ VSYNFRS
//
