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Database: UniProt
Entry: A7H629_CAMJD
LinkDB: A7H629_CAMJD
Original site: A7H629_CAMJD 
ID   A7H629_CAMJD            Unreviewed;       254 AA.
AC   A7H629;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000256|ARBA:ARBA00041694};
DE   AltName: Full=DPNPase {ECO:0000256|ARBA:ARBA00042530};
GN   Name=cysQ {ECO:0000313|EMBL:ABS43484.1};
GN   OrderedLocusNames=JJD26997_2054 {ECO:0000313|EMBL:ABS43484.1};
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109 {ECO:0000313|EMBL:ABS43484.1, ECO:0000313|Proteomes:UP000002302};
RN   [1] {ECO:0000313|Proteomes:UP000002302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97
RC   {ECO:0000313|Proteomes:UP000002302};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000768; ABS43484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H629; -.
DR   KEGG; cjd:JJD26997_2054; -.
DR   HOGENOM; CLU_044118_3_0_7; -.
DR   OMA; SADCYPR; -.
DR   Proteomes; UP000002302; Chromosome.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01638; CysQ; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   PANTHER; PTHR43028:SF5; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABS43484.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   254 AA;  29058 MW;  AC126BDE3EE50AB7 CRC64;
     MLNLDKFLQI AINASNQASK AILEERKNFK TWEKEDKSPL TSADLASNKI LNDILGSTDI
     KILSEEKLLS KEECEELKTF WLIDPLDGTS GFLKGSDEFC VMISLVHDNR PVLSLIQNPS
     KDDIFYAHAK TKVYKNDKLL QINQQEYEKN KYKALLSVNH LSKDDEDFAK EHQLEAINIG
     SGLKFCAILE AKAGVYKRFE KLNIWDIVAG DFLINQNGGF MGDFSKKYIL YHPLNYRSSP
     FICVSSRNFL QDFL
//
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