(data stored in SCRATCH zone)

SWISSPROT: A0KFU1_AERHH

ID   A0KFU1_AERHH            Unreviewed;       270 AA.
AC   A0KFU1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000256|HAMAP-Rule:MF_02095};
DE            EC=3.1.3.7 {ECO:0000256|HAMAP-Rule:MF_02095};
DE   AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_02095};
DE   AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_02095};
DE            Short=PAP phosphatase {ECO:0000256|HAMAP-Rule:MF_02095};
GN   Name=cysQ-1 {ECO:0000313|EMBL:ABK35844.1};
GN   Synonyms=cysQ {ECO:0000256|HAMAP-Rule:MF_02095};
GN   OrderedLocusNames=AHA_0584 {ECO:0000313|EMBL:ABK35844.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK35844.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK35844.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
CC       {ECO:0000256|HAMAP-Rule:MF_02095}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02095};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02095};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02095}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02095}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_02095}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       CysQ family. {ECO:0000256|HAMAP-Rule:MF_02095}.
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DR   EMBL; CP000462; ABK35844.1; -; Genomic_DNA.
DR   RefSeq; WP_011704554.1; NC_008570.1.
DR   RefSeq; YP_855117.1; NC_008570.1.
DR   STRING; 380703.AHA_0584; -.
DR   EnsemblBacteria; ABK35844; ABK35844; AHA_0584.
DR   GeneID; 4489251; -.
DR   KEGG; aha:AHA_0584; -.
DR   PATRIC; fig|380703.7.peg.580; -.
DR   eggNOG; ENOG4108RNI; Bacteria.
DR   eggNOG; COG1218; LUCA.
DR   HOGENOM; HOG000282237; -.
DR   KO; K01082; -.
DR   OMA; VFHTSEV; -.
DR   BioCyc; AHYD380703:G1G7B-585-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_02095; CysQ; 1.
DR   InterPro; IPR006240; CysQ.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   TIGRFAMs; TIGR01331; bisphos_cysQ; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFU1.
DR   SWISS-2DPAGE; A0KFU1.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095,
KW   ECO:0000313|EMBL:ABK35844.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02095};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   REGION       91     94       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02095}.
FT   METAL        69     69       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        89     89       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        89     89       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL        91     91       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02095}.
FT   METAL        92     92       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   METAL       218    218       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING      69     69       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
FT   BINDING     218    218       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02095}.
SQ   SEQUENCE   270 AA;  29452 MW;  F508724AFBCE253B CRC64;
     MQELLAWVPG VKEIAREAGR ILHEIYHGGQ FERQLKEDAT PVTSADLAAD AYLKQALSAL
     TPHVPVLTEE AADIPFSQRA NWRQYWLVDP LDGTGEFIAG SGDFATLIAL VQDNVPVLGV
     IYAPESNVLY WAVRGHGAFK EANGEVHPIS AMHHEHDQPD SLVVAISRRQ KLENLTRRLN
     PAINYELIPL GSSSLKSCLV AEGAADCYVR LGPTGEWDTA AAQCIVEAAG GRILSLALQP
     LRYNETESLE NPDFIVMGDP DLAWGSILAH
//

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