ID A0A1H6A6C4_9ACTN Unreviewed; 481 AA.
AC A0A1H6A6C4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05444920_1021039 {ECO:0000313|EMBL:SEG43922.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEG43922.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEG43922.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEG43922.1,
RC ECO:0000313|Proteomes:UP000236732};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNVT01000002; SEG43922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6A6C4; -.
DR Proteomes; UP000236732; 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; cd02205; CBS_pair_SF; 1.
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; IPR000644; CBS_dom.
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; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; 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|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_02250}; Reference proteome {ECO:0000313|Proteomes:UP000236732}.
FT DOMAIN 96..155
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 156..212
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 305
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 248..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 248..250
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 298..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
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 302
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 305
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 481 AA; 51013 MW; 52BBC68A3C82FD10 CRC64;
MNVRFLNDLE PQYDLTYSDV FMVPSRSSIG SRLAVDLSTN DGTGTTIPIV VANMTAVAGR
RMAETVARRG GITVIPQDIP MDVVANVVDW VKKRDLVHDT PLTLTSHATV GEALQLLPKR
AHGAVIVVDW QNRPVGVVTT ADCQGVDMFT QLSQVMSSEP LTLPAGLDPH LAFERLHGGR
HRLAPVVDEE GRLVGILTRT GALRATLYQP AVDAGGRLRI AAAVGVNGDV AAKAKELLEA
GIDCLVVDTA HGHQEKMIAA LRAVTALDPG VPVAAGNVVT AAGVRDLVDA GADILKVGVG
PGAMCTTRMM TGVGRPQFSA VLECSAEARR LGRHVWADGG VRHPRDVALA LAAGASNVMI
GSWFAGTYES PGDTHTDAKG REYKENYGMA SARAVRLRTA EDSAFERARK ALFEEGISTS
RMYLDPKRPS VEDQIDAIVA GLRSSCTYAG AATLEEFHAQ AVVGVQSSSG YAEGMPLHQS
W
//
