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Database: UniProt
Entry: A0A239HK30_9ACTN
LinkDB: A0A239HK30_9ACTN
Original site: A0A239HK30_9ACTN 
ID   A0A239HK30_9ACTN        Unreviewed;       478 AA.
AC   A0A239HK30;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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=SAMN06265355_13213 {ECO:0000313|EMBL:SNS81710.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS81710.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNS81710.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS81710.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNP01000032; SNS81710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239HK30; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000198420; 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; 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|HAMAP-Rule:MF_02250};
KW   Potassium {ECO:0000256|PIRSR:PIRSR000130-4};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_02250}.
FT   DOMAIN          153..211
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        302
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT   BINDING         245..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         245..247
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT   BINDING         295..297
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         295..297
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02250"
FT   BINDING         297
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         299
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"
SQ   SEQUENCE   478 AA;  50323 MW;  99C4EA24DFA5182F CRC64;
     MHLLNGERSA HDLTYNDVFM VPRRSSVGSR LEVDLATSDG SGTTIPLVVA NMTAVSGRRM
     AETAARRGGV AVLPQDIPVD VVAEVIDWVK GRDLVVDTAI RLGPSSTAGD ALALLPKRAH
     NAVIVVEDDR PVGVVTEADC MGVDRFAQLR DIMSRDLVTL PAGVDPREAF NRLHERGHRL
     APVVDAEGRL AGVLTRTGAL RATLYRPAVD AGGRLRVAAA VGVNGDVAGK AKALLAAGAD
     LLVVDTAHGH QDKMISALAA VRALDPAVPV VAGNVVTAEG TRELIEAGAD IVKVGVGPGA
     MCTTRMMTGV GRPQFSAVLE CAAEARRLGR HVWADGGVRH PRDVALALAA GAANVMVGSW
     FAGTYESPGD LQRAADGRLY KESFGMASAR AVRLRTAEDS PFDRARKALF EEGISASRMF
     LDPQRPGVED LIDSIVAGLR SSCTYAGART LEEFHERATI GIQSPSGYAE GKPLSSSW
//
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