ID   GUAB1_MYCTO             Reviewed;         479 AA.
AC   P9WKI2; L0TAS0; P65172; Q50591;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_02250};
DE            EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_02250};
DE   AltName: Full=Guanosine 5'-monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_02250};
DE            Short=GMPR {ECO:0000255|HAMAP-Rule:MF_02250};
GN   Name=guaB1 {ECO:0000255|HAMAP-Rule:MF_02250}; OrderedLocusNames=MT1891;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in the purine-salvage pathway. Catalyzes the NADPH-
CC       dependent conversion of GMP to IMP. {ECO:0000255|HAMAP-Rule:MF_02250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC         Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02250};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17187;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02250};
CC   -!- COFACTOR:
CC       Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02250}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaB1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02250}.
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DR   EMBL; AE000516; AAK46162.1; -; Genomic_DNA.
DR   PIR; C70664; C70664.
DR   RefSeq; WP_003902189.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKI2; -.
DR   SMR; P9WKI2; -.
DR   EnsemblBacteria; AAK46162; AAK46162; MT1891.
DR   KEGG; mtc:MT1891; -.
DR   PATRIC; fig|83331.31.peg.2035; -.
DR   HOGENOM; CLU_022552_2_1_11; -.
DR   UniPathway; UPA00591; -.
DR   Proteomes; UP000001020; Chromosome.
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; -; 1.
DR   HAMAP; MF_02250; GMPR_GuaB1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR005991; IMP_DH-rel1.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01303; IMP_DH_rel_1; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
KW   CBS domain; NADP; Oxidoreductase; Purine salvage; Repeat.
FT   CHAIN           1..479
FT                   /note="GMP reductase"
FT                   /id="PRO_0000427649"
FT   DOMAIN          96..153
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT   DOMAIN          154..212
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT   ACT_SITE        303
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT   BINDING         246..248
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT   BINDING         296..298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
SQ   SEQUENCE   479 AA;  49965 MW;  F34DAB1E6806B463 CRC64;
     MMRFLDGHPP GYDLTYNDVF IVPNRSEVAS RFDVDLSTAD GSGTTIPVVV ANMTAVAGRR
     MAETVARRGG IVILPQDLPI PAVKQTVAFV KSRDLVLDTP VTLAPDDSVS DAMALIHKRA
     HGVAVVILEG RPIGLVRESS CLGVDRFTRV RDIAVTDYVT APAGTEPRKI FDLLEHAPVD
     VAVLTDADGT LAGVLSRTGA IRAGIYTPAT DSAGRLRIGA AVGINGDVGA KARALAEAGV
     DVLVIDTAHG HQVKTLDAIK AVSALDLGLP LAAGNVVSAE GTRDLLKAGA NVVKVGVGPG
     AMCTTRMMTG VGRPQFSAVL ECASAARQLG GHIWADGGIR HPRDVALALA AGASNVMIGS
     WFAGTYESPG DLMRDRDDQP YKESYGMASK RAVVARTGAD NPFDRARKAL FEEGISTSRM
     GLDPDRGGVE DLIDHITSGV RSTCTYVGAS NLAELHERAV VGVQSGAGFA EGHPLPAGW