ID A0A2A9DZQ9_9MICO Unreviewed; 374 AA.
AC A0A2A9DZQ9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=IMP dehydrogenase {ECO:0000313|EMBL:PFG32083.1};
GN ORFNames=ATJ78_3067 {ECO:0000313|EMBL:PFG32083.1};
OS Microbacterium agarici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=630514 {ECO:0000313|EMBL:PFG32083.1, ECO:0000313|Proteomes:UP000221369};
RN [1] {ECO:0000313|EMBL:PFG32083.1, ECO:0000313|Proteomes:UP000221369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21798 {ECO:0000313|EMBL:PFG32083.1,
RC ECO:0000313|Proteomes:UP000221369};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PFG32083.1}.
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DR EMBL; PDJE01000001; PFG32083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9DZQ9; -.
DR Proteomes; UP000221369; Unassembled WGS sequence.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR005992; IMP_DH-rel2.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01304; IMP_DH_rel_2; 1.
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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000221369}.
FT DOMAIN 17..300
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
SQ SEQUENCE 374 AA; 39811 MW; FAA1411160EFE7CB CRC64;
MSQETEIGRA KRARTTFSFD DVAIVPSRRT RDPEDVSTAW TIDAYTFDTP FIAAPMDSVV
SPRTAIMMGQ LGGLGVLDLE GLWTRYENPE PILDEIRSMP ADAVVARMQE LYAEPIKAEL
ITARLEEIRE SGVTVAGSLS PQRTQEFYQT VVDAGVDLFV IRGTTVSAEH VSQNQEPLNL
KKFIYELDVP VIVGGAATYT AALHLMRTGA AGVLVGFGGG AASTTRNTLG IHAPMATAVA
DVAGARRDYL DESGGRYVHV IADGGLGTSG DIVKAIACGA DAVMLGTTLA RASDAPGGGF
HWGAEAHHSK LPRGNRVEVG TTGTLEEIIY GPATTPDGTA NLLGALKRSM ATTGYSDLKE
FQRVEVVVAP YRLR
//