ID A0A0M2M2P0_9MICO Unreviewed; 502 AA.
AC A0A0M2M2P0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_02250};
DE EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_02250};
DE AltName: Full=Guanosine 5'-monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_02250};
DE Short=GMPR {ECO:0000256|HAMAP-Rule:MF_02250};
GN Name=guaB1 {ECO:0000256|HAMAP-Rule:MF_02250};
GN ORFNames=XM48_02790 {ECO:0000313|EMBL:KKI22149.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI22149.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI22149.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI22149.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the purine-salvage pathway. Catalyzes the NADPH-
CC dependent conversion of GMP to IMP. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_02250};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02250};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway.
CC {ECO:0000256|HAMAP-Rule:MF_02250}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaB1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02250}.
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:KKI22149.1}.
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DR EMBL; LAYO01000068; KKI22149.1; -; Genomic_DNA.
DR RefSeq; WP_046454263.1; NZ_LAYO01000068.1.
DR AlphaFoldDB; A0A0M2M2P0; -.
DR STRING; 1642040.XM48_02790; -.
DR PATRIC; fig|1642040.3.peg.1572; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02250; GMPR_GuaB1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005991; GUAB1.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01303; IMP_DH_rel_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02250};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02250}; Potassium {ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_02250};
KW Reference proteome {ECO:0000313|Proteomes:UP000033836}.
FT DOMAIN 11..496
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 326
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 269..271
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 319..321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 319..321
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 321
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 326
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
SQ SEQUENCE 502 AA; 51404 MW; EF7D9F47D5157B25 CRC64;
MQISGQPTGD LTYSDVFLIP RRSAVGSRFA VDLAPGDGTP ATIPLVAANM NSVSGPRLAA
TLARRGGLAV LPQDPPLPVV EEAIRWVKER PASCDAPIVA GAGDTAADAL RRVPPSEQHG
LVVVRGDAER YADGTAVASG APVGIPVAEV LGILPAHRLA SVPEDARLGD LVRGELPTIP
AAELGEGRAA FDAVLAAEEA LGTPLLCVLE GDRVVGTITS RSALRNALYA PAVDRDGRLA
VAAAVGINGD VAGKASALAA AGADVLVVDT AHGHQEGMIR ALRTIADLDL GLPVAAGNIV
TADGVHDLVN AGATILKVGV GPAAMCTTRM MTAVGRPQFS AVLETAEAAS ELGAHVWADG
GVRYPRDVAL ALAAGAASIM IGSWFAGTIE APGELVADPG GRLYKESWGM ASTKAVQARF
GGLDPYERAR KELFAEGISS SKIYLDPQRP SVEDLVDMIT SGVRSSFTYA GAGSVAEFHE
RAHVGLQSAA GYEEGKALPV SW
//
