ID A0A239B864_9ACTN Unreviewed; 220 AA.
AC A0A239B864;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=GDP-mannose pyrophosphatase {ECO:0000256|ARBA:ARBA00016377};
DE AltName: Full=GDP-mannose hydrolase {ECO:0000256|ARBA:ARBA00032162};
DE AltName: Full=GDPMK {ECO:0000256|ARBA:ARBA00032272};
GN ORFNames=SAMN04488107_0967 {ECO:0000313|EMBL:SNS03508.1};
OS Geodermatophilus saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNS03508.1, ECO:0000313|Proteomes:UP000198386};
RN [1] {ECO:0000313|EMBL:SNS03508.1, ECO:0000313|Proteomes:UP000198386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45423 {ECO:0000313|EMBL:SNS03508.1,
RC ECO:0000313|Proteomes:UP000198386};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + H2O = alpha-D-mannose 1-phosphate + GMP
CC + 2 H(+); Xref=Rhea:RHEA:27978, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58115, ChEBI:CHEBI:58409;
CC Evidence={ECO:0000256|ARBA:ARBA00000847};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR604385-2};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudK subfamily.
CC {ECO:0000256|ARBA:ARBA00007275}.
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DR EMBL; FZOH01000002; SNS03508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239B864; -.
DR OrthoDB; 5292471at2; -.
DR Proteomes; UP000198386; Unassembled WGS sequence.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03424; ADPRase_NUDT5; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR004385; NDP_pyrophosphatase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR NCBIfam; TIGR00052; nudix-type nucleoside diphosphatase, YffH/AdpP family; 1.
DR PANTHER; PTHR11839:SF18; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2}.
FT DOMAIN 69..208
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 112..133
FT /note="Nudix box"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 220 AA; 23847 MW; 0B82425F5BA87A31 CRC64;
MTGVVGVDLP DARGRTGLDR AGRDLTGNPD VVVRDVEVLS SSWYVNRRTT FDRRGRDGVW
RTERRETHDR GNGATVLLYD TARRTVLLTR QFRFPAYVNG SPDGVLVETA AGLLDEQDAE
AAVRREAAEE LGVAVGPLTR LPDVWMSPGS VTERLAFFAG PYTPADRVSA GGGLAEEGED
IEVLELPVEQ ALAMVDDGRI ADAKTVLLLQ WAALRGPFAA
//
