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Database: UniProt
Entry: A0A1P8UG93_9GAMM
LinkDB: A0A1P8UG93_9GAMM
Original site: A0A1P8UG93_9GAMM 
ID   A0A1P8UG93_9GAMM        Unreviewed;       258 AA.
AC   A0A1P8UG93;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=HAD family hydrolase {ECO:0000313|EMBL:APZ42835.1};
GN   ORFNames=BW247_06790 {ECO:0000313|EMBL:APZ42835.1};
OS   Acidihalobacter ferrooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ42835.1, ECO:0000313|Proteomes:UP000243807};
RN   [1] {ECO:0000313|EMBL:APZ42835.1, ECO:0000313|Proteomes:UP000243807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V8 {ECO:0000313|EMBL:APZ42835.1,
RC   ECO:0000313|Proteomes:UP000243807};
RA   Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA   Watkin E.L.J.;
RT   "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT   V8).";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP019434; APZ42835.1; -; Genomic_DNA.
DR   RefSeq; WP_076836484.1; NZ_CP019434.1.
DR   AlphaFoldDB; A0A1P8UG93; -.
DR   STRING; 1765967.BW247_06790; -.
DR   OrthoDB; 367448at2; -.
DR   Proteomes; UP000243807; Chromosome.
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; IPR041492; HAD_2.
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; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:APZ42835.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243807}.
FT   COILED          98..125
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   258 AA;  30454 MW;  68F67DB86EBBF766 CRC64;
     MSIRAVLFDL YGTLIHIETD ESQGEIYWAI ARYLSYHRIR IDADALRERY FELAKRQKRD
     SGERYPEMDA RAVWRAILSD GTRHYRPEAF AGEGPDKQRE VEKRRERLAR ELVRLQRALS
     RRQIERYPGA KHLLQSIAAD YRLGIVSDAQ HDFARAEMRI TKLRKYFPVK TISDEFGYRK
     PDPRLFQQTC AALEVLPEET IYVGNDMYRD IYGAHQAGLR TILVWSDQGR KEYRDTRADY
     DARDLFQVLE GIRFLAAQ
//
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