LOCUS WP_120189242 709 aa linear BCT 15-JUL-2025
DEFINITION HD family phosphohydrolase [Ammoniphilus oxalaticus].
ACCESSION WP_120189242
VERSION WP_120189242.1
KEYWORDS RefSeq.
SOURCE Ammoniphilus oxalaticus
ORGANISM Ammoniphilus oxalaticus
Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
Paenibacillaceae; Aneurinibacillus group; Ammoniphilus.
REFERENCE 1 (residues 1 to 709)
AUTHORS Huynh,T.N., Luo,S., Pensinger,D., Sauer,J.D., Tong,L. and
Woodward,J.J.
TITLE An HD-domain phosphodiesterase mediates cooperative hydrolysis of
c-di-AMP to affect bacterial growth and virulence
JOURNAL Proc Natl Acad Sci U S A 112 (7), E747-E756 (2015)
PUBMED 25583510
REFERENCE 2 (residues 1 to 709)
AUTHORS Aravind,L. and Koonin,E.V.
TITLE The HD domain defines a new superfamily of metal-dependent
phosphohydrolases
JOURNAL Trends Biochem Sci 23 (12), 469-472 (1998)
PUBMED 9868367
COMMENT REFSEQ: This record represents a single, non-redundant, protein
sequence which may be annotated on many different RefSeq genomes
from the same, or different, species.
##Evidence-For-Name-Assignment-START##
Evidence Category :: Conserved Domain (CDD)
Evidence Accession :: Domain architecture ID 11445215
Evidence Source :: NCBI SPARCLE
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..709
/organism="Ammoniphilus oxalaticus"
/db_xref="taxon:66863"
Protein 1..709
/product="HD family phosphohydrolase"
/EC_number="3.1.4.59"
/GO_function="GO:0000166 - nucleotide binding [Evidence
IEA]"
/GO_function="GO:0016787 - hydrolase activity [Evidence
IEA]"
/GO_function="GO:0046872 - metal ion binding [Evidence
IEA]"
/GO_function="GO:0106409 - cyclic-di-AMP phosphodiesterase
activity [Evidence IEA]"
/calculated_mol_wt=79649
Region 17..707
/region_name="PgpH"
/note="Cyclic di-AMP-specific phosphodiesterase PgpH, HD
superfamily [Signal transduction mechanisms]; COG1480"
/db_xref="CDD:441089"
ORIGIN
1 mkkrllqsvq ripnnwktsr amrallfvll aiaiyfllle hvipktydlq rnmisdvlvt
61 apmevedtes tkklqgdaik avspiytmde riianqlkvl dqifrdvtdv klkreeesal
121 tnsseqqqdk eklkelvpyn fsdetyqtll kqtpeslatm kaisrnivss imlegfrsge
181 evkvkdrvte qlttselesr mvqaireval atvvpnivfd eqateqakdr varsvkpvii
241 hkgeilvgeg eyitdeiyrk lgvagllthn pnyypyigla lfvslavvff hlyiskgale
301 irvnntqllm fiviillnlv vlktvslgkd leysfigfla pvafgsmliv lfidyhlalf
361 agglfsicas lmfnssseyl fnygygfval aacvtgaycl hnrtkrrnil laglfvvftn
421 iisvtsiyml fysvkwaelf qlygfaitsg llasiltigf vpflessfgi lssmkliels
481 spnqpllrrl lmetpgtyhh simvanlsea aaeaigangl larvgayyhd vgkmkrpqff
541 ienqmggenp hdkqaptlsr tiilshtedg vkllqeynlp kpiqdiaaqh hgtsllrffy
601 hkatqeatrp iseeefrypg pkpqfkeaai vgicdsveaa vrslakpspe qienlvrkiv
661 kdrlddrqls ecdltflele qitqsicetl kgifhtriey paeaevkha
//