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Database: UniProt
Entry: W7E612_9PROT
LinkDB: W7E612_9PROT
Original site: W7E612_9PROT 
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
//
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