GUAB1_MYCBO
ID GUAB1_MYCBO Reviewed; 479 AA.
AC P65173; A0A1R3XZH2; Q50591; X2BJ81;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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, ECO:0000312|EMBL:SIU00478.1};
GN OrderedLocusNames=BQ2027_MB1874C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SIU00478.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LT708304; SIU00478.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_855526.1; NC_002945.3.
DR RefSeq; WP_003902189.1; NC_002945.4.
DR AlphaFoldDB; P65173; -.
DR SMR; P65173; -.
DR EnsemblBacteria; SIU00478; SIU00478; BQ2027_MB1874C.
DR PATRIC; fig|233413.5.peg.2054; -.
DR OMA; TYDDVFM; -.
DR UniPathway; UPA00591; -.
DR Proteomes; UP000001419; 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_0000093786"
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
