ID Q03YG4_LEUMM Unreviewed; 380 AA.
AC Q03YG4;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000313|EMBL:ABJ61758.1};
DE EC=1.1.1.205 {ECO:0000313|EMBL:ABJ61758.1};
GN OrderedLocusNames=LEUM_0645 {ECO:0000313|EMBL:ABJ61758.1};
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ61758.1, ECO:0000313|Proteomes:UP000000362};
RN [1] {ECO:0000313|EMBL:ABJ61758.1, ECO:0000313|Proteomes:UP000000362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO
RC 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y
RC {ECO:0000313|Proteomes:UP000000362};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR EMBL; CP000414; ABJ61758.1; -; Genomic_DNA.
DR RefSeq; WP_011679454.1; NC_008531.1.
DR AlphaFoldDB; Q03YG4; -.
DR EnsemblBacteria; ABJ61758; ABJ61758; LEUM_0645.
DR GeneID; 61176879; -.
DR KEGG; lme:LEUM_0645; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_0_9; -.
DR Proteomes; UP000000362; Chromosome.
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; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR013785; Aldolase_TIM.
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 SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ABJ61758.1};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 14..360
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
SQ SEQUENCE 380 AA; 39955 MW; 4A63D9180919F28D CRC64;
MQKFSSTNKF VPMGLTFEDV KLVDDLQSTV TPESVSVTTS LTPTLKLNIP LLSAAMDTVT
EARFATALAK LGGLGVIHKN MTISAQADEV RKVKTATFDS ADFPNAAVDA KGHLLVAGAV
GVTNDTVDRV QAMVEAGADA IVLDSAHGHS EGVLRKVSEV RSTFPNLNII AGNIATREGA
AALYDAGADV VKIGIGPGSI CTTRVVAGIG VPQVSAIRDA ALEAAARGKK IIADGGVKTS
LDIVKAISAG GNAVMLGSMF SGTEETPGEV FEDNGQKYKT YRGMGSIAAM ENGSKDRYFQ
GEVNEAKKMV PEGIEARVTY KGDLTTILNA MLVDIHKKMA QLGETTIDDL VNHEHIARDS
EVFDFEAATD KQKPVVAAQF
//
