GUAB1_MYCLE
ID GUAB1_MYCLE Reviewed; 478 AA.
AC O32912;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=ML2066;
GN ORFNames=MLCB1788.20;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL008609; CAA15452.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC31021.1; -; Genomic_DNA.
DR PIR; T44751; T44751.
DR RefSeq; NP_302378.1; NC_002677.1.
DR RefSeq; WP_010908698.1; NC_002677.1.
DR AlphaFoldDB; O32912; -.
DR SMR; O32912; -.
DR STRING; 272631.ML2066; -.
DR EnsemblBacteria; CAC31021; CAC31021; CAC31021.
DR KEGG; mle:ML2066; -.
DR PATRIC; fig|272631.5.peg.3887; -.
DR Leproma; ML2066; -.
DR eggNOG; COG0516; Bacteria.
DR eggNOG; COG0517; Bacteria.
DR HOGENOM; CLU_022552_2_1_11; -.
DR OMA; TYDDVFM; -.
DR UniPathway; UPA00591; -.
DR Proteomes; UP000000806; 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; 2.
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; Reference proteome;
KW Repeat.
FT CHAIN 1..478
FT /note="GMP reductase"
FT /id="PRO_0000093787"
FT DOMAIN 95..152
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT DOMAIN 153..211
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT ACT_SITE 302
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT BINDING 245..247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
FT BINDING 295..297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02250"
SQ SEQUENCE 478 AA; 50383 MW; B52010A46E7A55F4 CRC64;
MRFLDGHQPR FDLTYKDVFI VPHRSDVASR FDVDLSTYDG SGTTIPVVVA NMTTVAGQRM
AETVARRGGL VILPQDLPIA TVQQAVEFVK SRDLVIDTPV LLTPNDSVSD ATTLIHKRAH
GVAVVAFEGR PIGLVRESSC LGVDRFTRVR DVATTDFVTA PVGTDPRKIF DLLEHAPIDV
AVLTNADGTL AGVLTRTGAI RAGIYTPATD ARGRLRIGAA VGINGDVAGK AQSLAEAGVD
VLVVDTAHGY QVKTLEAIKC VASLNLGVPL VAGNVVSAEG TRELLNAGAT IVKVGVGPGA
MCTTRMMTGV GRPQFSAVLE CASAARKLNR HVWADGGVRH PRDVALALAA GASNVMIGSW
FAGTYESPGD LMRDRHDQPY KESYGMASKR AVVARTVADS SFDRARKALF DEGISTSRMG
LDPDHGGVED LIDHITSGVR STCTYVGAST LAELHEKAVV GVQSAAGFAE GHPLPSGW
