ID A0A1X3PAX4_9MICC Unreviewed; 501 AA.
AC A0A1X3PAX4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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=BCY76_002470 {ECO:0000313|EMBL:OSM44396.1};
OS Nesterenkonia sp. PF2B19.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=1881858 {ECO:0000313|EMBL:OSM44396.1, ECO:0000313|Proteomes:UP000175621};
RN [1] {ECO:0000313|EMBL:OSM44396.1, ECO:0000313|Proteomes:UP000175621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF2B19 {ECO:0000313|EMBL:OSM44396.1,
RC ECO:0000313|Proteomes:UP000175621};
RX PubMed=28408669;
RA Singh P., Kapse N., Roy U., Singh S.M., Dhakephalkar P.K.;
RT "Draft Genome Sequence of Permafrost Bacterium Nesterenkonia sp. Strain
RT PF2B19, Revealing a Cold Adaptation Strategy and Diverse Biotechnological
RT Potential.";
RL Genome Announc. 5:e00133-17(2017).
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:OSM44396.1}.
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DR EMBL; MDSS02000005; OSM44396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3PAX4; -.
DR STRING; 1881858.BCY76_002470; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000175621; 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; 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.
DR PROSITE; PS51371; CBS; 1.
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}.
FT DOMAIN 93..151
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 325
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 261..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 261..263
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 318..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 318..320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 320
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 322
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 325
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 501 AA; 53113 MW; 94E262515DC94909 CRC64;
MKFLNEPTTD LTYADVFLVP SRSEAMSRME VDISADDGTG STIPLVAANM TAVTGRRMVE
TMARRGGLGV LPQDIPLEVI RQVTEWVKSC HPVFETPLKV GPQDTILDVL HLLDKRNHRS
VCVVDEDLRL AGIVTAEDGE GRDRFSSVGS VMRMPQVRFT TAELGLQDQA GAQDAEALDA
GLRQAFLAMD ELGCDYAPVT TSDGTLAGVL TPRGALRSTL FAPNLDSAGR LKVAAAVGIN
GDVAGRAESL LDAGVDVLVV DTAHGHQRKM FEALRAVRAV VDSHAEGGLT VPVVAGNVVT
PEGVRDLVAA GADIVKVGVG PGAMCTTRMM TAVGRPQFSA VLECAAAARE LGRHIWADGG
VRHPRDIALA LAAGASQVMV GSWFAGTFES PGDLIAEADG RRYKESYGMA SARAVQHRTA
GEDAFSRARK SLFEEGISTS KMYLDPQRPG VEDLLDSITA GVRSSMTYAG ARDLPRFREQ
AVAGVQSAAG YEEGKPVPTT W
//
