ID T2SPA3_HELPX Unreviewed; 309 AA.
AC T2SPA3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Inosine 5'-monophosphate dehydrogenase {ECO:0000313|EMBL:EQD93354.1};
DE EC=1.1.1.205 {ECO:0000313|EMBL:EQD93354.1};
DE Flags: Fragment;
GN ORFNames=L934_06995 {ECO:0000313|EMBL:EQD93354.1};
OS Helicobacter pylori PZ5080.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1337394 {ECO:0000313|EMBL:EQD93354.1, ECO:0000313|Proteomes:UP000015663};
RN [1] {ECO:0000313|EMBL:EQD93354.1, ECO:0000313|Proteomes:UP000015663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PZ5080 {ECO:0000313|EMBL:EQD93354.1,
RC ECO:0000313|Proteomes:UP000015663};
RX PubMed=24051318;
RA Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT Regions of Low and High Gastric Cancer Risk in Colombia.";
RL Genome Announc. 1:e00736-13(2013).
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:EQD93354.1}.
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DR EMBL; ASYV01000096; EQD93354.1; -; Genomic_DNA.
DR AlphaFoldDB; T2SPA3; -.
DR Proteomes; UP000015663; 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 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 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};
KW Oxidoreductase {ECO:0000313|EMBL:EQD93354.1};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 92..148
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 152..209
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT NON_TER 309
FT /evidence="ECO:0000313|EMBL:EQD93354.1"
SQ SEQUENCE 309 AA; 33319 MW; B9549AFDB2908263 CRC64;
MRILQRALTF EDVLMVPRKS SVLPKDVSLK SRLTKNIRLN IPFISAAMDT VTEHKTAIAM
ARLGGIGIVH KNMDIQTQVK EIAKVKKSES GVINDPIFIQ AHRTLADAKA IADNYKISGV
PVVDDKGLLI GILTNRDVRF ETDLSKKVGD VMTKMPLVTA HVGISLDEAS DLMHKHKIEK
LPIVDKDNVL KGLITIKDIQ KRIEYPEANK DDFGRLRVGA AIGVGQLDRA EMLVKAGVDA
LVLDSAHGHS ANILHTLEEI KKSLVVDVIV GNVVTKEATS DLISAGADAV KVGIGPGSIC
TTRIVAGVG
//
