ID W7E612_9PROT Unreviewed; 202 AA.
AC W7E612;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=COMX_02270 {ECO:0000313|EMBL:EUK18536.1};
OS Commensalibacter papalotli (ex Servin-Garciduenas et al. 2014).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1208583 {ECO:0000313|EMBL:EUK18536.1, ECO:0000313|Proteomes:UP000019250};
RN [1] {ECO:0000313|EMBL:EUK18536.1, ECO:0000313|Proteomes:UP000019250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-MONARCH01 {ECO:0000313|Proteomes:UP000019250};
RX PubMed=24604647;
RA Servin-Garciduenas L.E., Sanchez-Quinto A., Martinez-Romero E.;
RT "Draft Genome Sequence of Commensalibacter papalotli MX01, a Symbiont
RT Identified from the Guts of Overwintering Monarch Butterflies.";
RL Genome Announc. 2:e00128-14(2014).
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|PIRSR:PIRSR604385-2};
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:EUK18536.1}.
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DR EMBL; ATSX01000001; EUK18536.1; -; Genomic_DNA.
DR RefSeq; WP_034336551.1; NZ_ATSX01000001.1.
DR AlphaFoldDB; W7E612; -.
DR STRING; 1208583.COMX_02270; -.
DR eggNOG; COG0494; Bacteria.
DR OrthoDB; 5292471at2; -.
DR Proteomes; UP000019250; 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:SF16; GDP-MANNOSE PYROPHOSPHATASE; 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 Hydrolase {ECO:0000313|EMBL:EUK18536.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000019250}.
FT DOMAIN 42..189
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 202 AA; 23051 MW; AED7985445714B7E CRC64;
MSKMILKETS TIYKGHSKLE LAQMLQQYDD GQEVLLSREV LKARDSVVVL LYRQDTKQLV
FTSQWRAPIV FCGDQRPVIE ACAGNIDQED FDSHPQDVLA AANIAVIREV QEETGWHIAK
LDYLYALYSC PGISTEKLYY YIACVDKRIQ QGGGLRSEGE DIFVLEMSLS EAIEKIKNEE
IIDLKTVALI QYLQIHKAVY LE
//