ID K2LZ21_BIFBI Unreviewed; 324 AA.
AC K2LZ21;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000313|EMBL:EKF15041.1};
DE Flags: Fragment;
GN ORFNames=B217_09150 {ECO:0000313|EMBL:EKF15041.1};
OS Bifidobacterium bifidum IPLA 20015.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1207543 {ECO:0000313|EMBL:EKF15041.1, ECO:0000313|Proteomes:UP000007366};
RN [1] {ECO:0000313|EMBL:EKF15041.1, ECO:0000313|Proteomes:UP000007366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPLA 20015 {ECO:0000313|EMBL:EKF15041.1,
RC ECO:0000313|Proteomes:UP000007366};
RA Gueimonde M., Margolles A., Sanchez B.;
RT "Genome sequence of Bifidobacterium bifidum IPLA 20015.";
RL Submitted (SEP-2012) 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:EKF15041.1}.
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DR EMBL; AMPM01000352; EKF15041.1; -; Genomic_DNA.
DR AlphaFoldDB; K2LZ21; -.
DR Proteomes; UP000007366; 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 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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 100..159
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 163..220
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT NON_TER 324
FT /evidence="ECO:0000313|EMBL:EKF15041.1"
SQ SEQUENCE 324 AA; 34788 MW; CDB81F170F2CB485 CRC64;
MQSYAPVPPI FSKLGLAYDD VLLLPNETDV IPSEVDTTTH LTREITMKVP TISAAMDTVT
ESEMAIAMAR NGGIGVLHRN LSIDDQAAQV DVVKRSESGM ITDPLTVNPD VTLADLDKLC
GKFHISGLPV VDKENRLVGI ITNRDMRFIP SEDYDHLKVK DVMTKENLIT GPANISKDDA
HRLLAQHKVE KLPLIDDNGK LAGLITVKDF VKTEQYPDAT KDEQGRLRVA AGIGFLGDAW
QRASALMEAG VDVLVVDTAN GEARLALDMI SRIKRDPAFR GVQVIGGNIA TRSGAQAMID
AGVDAVKIGV GPGSICTTRV VAGV
//
