ID A0A164B829_9MICO Unreviewed; 485 AA.
AC A0A164B829;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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 ECO:0000313|EMBL:KZE88982.1};
GN ORFNames=AVP41_01773 {ECO:0000313|EMBL:KZE88982.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE88982.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE88982.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE88982.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-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}.
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:KZE88982.1}.
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DR EMBL; LQGV01000003; KZE88982.1; -; Genomic_DNA.
DR RefSeq; WP_067163408.1; NZ_LQGV01000003.1.
DR AlphaFoldDB; A0A164B829; -.
DR STRING; 1775956.AVP41_01773; -.
DR PATRIC; fig|1775956.3.peg.1766; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000076535; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076535}.
FT DOMAIN 12..479
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 309
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 252..254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 252..254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 302..304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 302..304
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT BINDING 304
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 306
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 309
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 485 AA; 50686 MW; 3189BA17920E1A70 CRC64;
MQFSGARPQV DLTYSDVFLV PRRSAVTSRL DVDLAPGDGT TATLPLVASN MNSVTGPRLA
AALARRGGLG VLPQDMALQQ IDAAIRWVKD QPVVWDTPLV LPPEATVAEA ALLLPPTDGH
GIVVAVEREG RVHRDDVLGV VPAQRLGTAL SDARLGDLVR GRVASIDADD VTDARHAFDL
IVAAEAETVC VLHHGYLVGT LSQRTALRST LYRPAVDANG RLIVAAAVGI NGDVAGKARA
LVAAGVDVLV VDTAHGHQEG MLRALREVAA LDLGVPIAAG NIVTADGVAD LVDAGASILK
VGVGPGAMCT TRMMTAVGRP QFSAVLETAQ AAAERGAHVW ADGGVRYPRD VALALAAGAA
SVMIGSWFAG TLEAPGQLQT DEAGRVYKES WGMASTKAVH GRFGRLDPYE RARKELFAEG
ISSSRIYLDP LRPSVEDLVD MITSGVRSSF TYAGAATVAE FHERALVGLQ SAAGYEEGKA
LPVSW
//
