ID A0A178YAU1_SINSA Unreviewed; 197 AA.
AC A0A178YAU1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ATB98_16910 {ECO:0000313|EMBL:OAP44564.1};
OS Sinorhizobium saheli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=36856 {ECO:0000313|EMBL:OAP44564.1, ECO:0000313|Proteomes:UP000078507};
RN [1] {ECO:0000313|EMBL:OAP44564.1, ECO:0000313|Proteomes:UP000078507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 7837 {ECO:0000313|EMBL:OAP44564.1,
RC ECO:0000313|Proteomes:UP000078507};
RA Yan H., Chen W.;
RT "Ensifer anhuiense sp. nov., an effective nitrogen fixation bacterium with
RT Glycine soja.";
RL Submitted (NOV-2015) 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}.
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:OAP44564.1}.
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DR EMBL; LNQB01000073; OAP44564.1; -; Genomic_DNA.
DR RefSeq; WP_066874445.1; NZ_WITB01000195.1.
DR AlphaFoldDB; A0A178YAU1; -.
DR STRING; 36856.ATB98_16910; -.
DR OrthoDB; 5292471at2; -.
DR Proteomes; UP000078507; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000078507}.
FT DOMAIN 46..190
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 88..109
FT /note="Nudix box"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 197 AA; 21900 MW; F1D9AB76D7F2EF64 CRC64;
MTKHAERVRI IDRQNLWNGF ISLERITLEQ QMSDGSTARL VREVHDHGRA ATILLFDPER
QVVVLVRQIR IPVFLQGEPG YLIETPAGLL DGEAPEVAIC REAMEETGYE IESAVHLFDA
YMSPGSVTER TSFFLGRIDT SRKTAAGGGL MHEGEDIEVL EIPFEEACAM VGTGEICDAK
TIMLLQWAML NRASLPA
//
