Y1054_AQUAE
ID Y1054_AQUAE Reviewed; 261 AA.
AC O67153;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Uncharacterized metallophosphoesterase aq_1054;
DE EC=3.1.-.-;
GN OrderedLocusNames=aq_1054;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07116.1; -; Genomic_DNA.
DR PIR; F70390; F70390.
DR RefSeq; NP_213716.1; NC_000918.1.
DR RefSeq; WP_010880654.1; NC_000918.1.
DR AlphaFoldDB; O67153; -.
DR SMR; O67153; -.
DR STRING; 224324.aq_1054; -.
DR EnsemblBacteria; AAC07116; AAC07116; aq_1054.
DR KEGG; aae:aq_1054; -.
DR PATRIC; fig|224324.8.peg.817; -.
DR eggNOG; COG1408; Bacteria.
DR HOGENOM; CLU_025443_3_2_0; -.
DR InParanoid; O67153; -.
DR OMA; DIFPRVP; -.
DR OrthoDB; 1690667at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008758; F:UDP-2,3-diacylglucosamine hydrolase activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..261
FT /note="Uncharacterized metallophosphoesterase aq_1054"
FT /id="PRO_0000172850"
FT BINDING 43
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 261 AA; 29310 MW; 7191EC3566A0D5D3 CRC64;
MFIAVLLGAY SHLETYFLRV EKYTIETEKL PKGTEIKIMN ASDMHLGPVM REDRVEMVKR
VYEREKPDIL VATGDTVDGN MKNLDYLAQM LAELNPPLGK FAVLGNHEYY VGLNQSLDFL
RKAGFRVLRG EAVEINNFLV IAGVDDSDGK RLGYRVFTDE LEVLKNVDTK KYVILLKHKP
RIKREAIKYV DLVLSGHTHG GVLFFVGYTI LRLIFETDRG IKELAPGKYI IVSKGVGTGG
PPMRLLSPPD VVIVTIKGKG N