ID L9V3A2_NATMM Unreviewed; 251 AA.
AC L9V3A2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Haloacid dehalogenase {ECO:0000313|EMBL:ELY31492.1};
GN ORFNames=C500_06351 {ECO:0000313|EMBL:ELY31492.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ELY31492.1, ECO:0000313|Proteomes:UP000011543};
RN [1] {ECO:0000313|EMBL:ELY31492.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00007958}.
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:ELY31492.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOHS01000026; ELY31492.1; -; Genomic_DNA.
DR AlphaFoldDB; L9V3A2; -.
DR PATRIC; fig|547559.17.peg.1230; -.
DR Proteomes; UP000011543; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.120.710; Haloacid dehalogenase hydrolase-like domain; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR PANTHER; PTHR46470:SF2; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 251 AA; 27339 MW; 5EF1A3773F17DBBD CRC64;
MERITTKRSE PSRSYVHTMA AYDAIYFDLD STLCEPIQDP DTLLAGTFDD AGIEPFCTPA
DLRAAIPDLP TAETAREFYE SLFSTVATQA EPHVQDRLGS DGPAELAAAY LEREDPTAVE
FRPGAKTALE FAREQGPVGL ITNGGRETQT QKLRALDIED AFDVRVFTDP AAGIFPKPDT
APFEYALREL EATPETAIHI GDSLHADVGG ANAIGLDSAW IELENQVQHG DPTVHQPTYE
LGTLESFEAI L
//
