ID A0A2W1YS32_9MICO Unreviewed; 479 AA.
AC A0A2W1YS32;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DEI94_14305 {ECO:0000313|EMBL:PZF45774.1};
OS Curtobacterium sp. MCBD17_040.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175674 {ECO:0000313|EMBL:PZF45774.1};
RN [1] {ECO:0000313|EMBL:PZF45774.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBD17_040 {ECO:0000313|EMBL:PZF45774.1};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-2018) 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:PZF45774.1}.
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DR EMBL; QKTL01000017; PZF45774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1YS32; -.
DR OrthoDB; 9805398at2; -.
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; IPR046342; CBS_dom_sf.
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; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
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}.
FT DOMAIN 12..474
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 303
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 246..248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 246..248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 296..298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 296..298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 298
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 300
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 303
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 479 AA; 49732 MW; 2528098F10AE220A CRC64;
MRFYETRPTH DLTYSDVFLV PSRSGVSSRF DVDLTPPDGT GATIPVVSAN MNSVTGPRLA
ATLARRGGLG VLPQDMHPQD LDAAIRWVKA QPVDHDTPVT MTPDTTVAEA LTQLAPVPGH
GVVVQDAGGE YLGCVPAVRL ATAGEDATVG DLLHGAVTAI DADDVDSPRA VFDLLAAAEV
DFAPVLRHGR VVGTTSPTSA IRSGIYRPAV DADGRLRVAA AVGINGDVAR KASALVAAGV
DVLVLDTAHG HQEGMLRALR TVADLGLGVP LVAGNVVTAD AVTHLVDAGA SIIKVGVGPG
AMCTTRMMTA VGRPQFSAVL ETAAAARALG AHVWADGGVR YPRDVALALA AGAASVMIGS
WFAGTVEAPG VLKVDAQGRR YKESWGMASA KAVRERFERL DPYERARKAL FAEGISSSTI
YLDPERPSVE DLLDMITAGV RSSATYAGAR DLPAFADRAL VGIQSAAGYE EGKPVPVSW
//
