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Database: UniProt
Entry: A0A2N6UQI0_9ACTO
LinkDB: A0A2N6UQI0_9ACTO
Original site: A0A2N6UQI0_9ACTO 
ID   A0A2N6UQI0_9ACTO        Unreviewed;       375 AA.
AC   A0A2N6UQI0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=GuaB3 family IMP dehydrogenase-related protein {ECO:0000313|EMBL:PMC85768.1};
GN   ORFNames=CJ187_03560 {ECO:0000313|EMBL:PMC85768.1};
OS   Gleimia hominis.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Gleimia.
OX   NCBI_TaxID=595468 {ECO:0000313|EMBL:PMC85768.1};
RN   [1] {ECO:0000313|EMBL:PMC85768.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMB0859 {ECO:0000313|EMBL:PMC85768.1};
RA   Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT   "Bacterial strain isolated from the female urinary microbiota.";
RL   Submitted (SEP-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:PMC85768.1}.
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DR   EMBL; PNHU01000001; PMC85768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N6UQI0; -.
DR   OrthoDB; 9805398at2; -.
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;
FT   DOMAIN          16..298
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
SQ   SEQUENCE   375 AA;  40474 MW;  B2B8DB3F57C74899 CRC64;
     MSYEIEIGRG KRARRAYTLD DVALVPARRT RDPEDVNVSW QIDAYHVQMP LLGAPMDSTM
     SPETAIELGR LGGIGVLDLE GLWTRYEDPQ PLLEEIRQLD AHASNARLQE IYSEPIKPEL
     MAARLGQLRD AGVVVAGKLS PQQTEKYWRY VVDAGVDLFV IRGTTVSAQH VSSRAQPLNL
     KRFIYELDVP VLVGGVATYT GALHLMRTGA AGVLVGFGGG AAHTTRQLLG IHAPMATAIA
     DVAAARRDYL DESGGRYVHI IADGGIGRSG DFIKAIGCGA DAVMIGAALA RAREAPGGGW
     HWGSEAYHPE LPRGQRVHVG TAGTMEQILL GPSSRADGKV NFIGSLRRAM ATTGYAEVKD
     LQRVEMVVSP YEKSL
//
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