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Database: UniProt
Entry: G0EDC7_PYRF1
LinkDB: G0EDC7_PYRF1
Original site: G0EDC7_PYRF1 
ID   G0EDC7_PYRF1            Unreviewed;       219 AA.
AC   G0EDC7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=HAD-superfamily hydrolase, subfamily IA, variant 3 {ECO:0000313|EMBL:AEM38612.1};
GN   OrderedLocusNames=Pyrfu_0743 {ECO:0000313|EMBL:AEM38612.1};
OS   Pyrolobus fumarii (strain DSM 11204 / 1A).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Pyrolobus.
OX   NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38612.1, ECO:0000313|Proteomes:UP000001037};
RN   [1] {ECO:0000313|EMBL:AEM38612.1, ECO:0000313|Proteomes:UP000001037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX   PubMed=21886865;
RA   Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA   Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA   Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT   Pyrolobus fumarii type strain (1A).";
RL   Stand. Genomic Sci. 4:381-392(2011).
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00007958}.
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DR   EMBL; CP002838; AEM38612.1; -; Genomic_DNA.
DR   RefSeq; WP_014026289.1; NC_015931.1.
DR   AlphaFoldDB; G0EDC7; -.
DR   STRING; 694429.Pyrfu_0743; -.
DR   GeneID; 25394833; -.
DR   KEGG; pfm:Pyrfu_0743; -.
DR   eggNOG; arCOG02291; Archaea.
DR   HOGENOM; CLU_1259141_0_0_2; -.
DR   InParanoid; G0EDC7; -.
DR   OrthoDB; 27736at2157; -.
DR   Proteomes; UP000001037; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR43611; ALPHA-D-GLUCOSE 1-PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR43611:SF3; FLAVIN MONONUCLEOTIDE HYDROLASE 1, CHLOROPLATIC; 1.
DR   Pfam; PF00702; Hydrolase; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AEM38612.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001037}.
SQ   SEQUENCE   219 AA;  24429 MW;  E342719B29B8FDBE CRC64;
     MPRNPTLLLD LGGVIYLTNE WYEETLYETA ARHLRALGAD ATPDSVRRVM DTWRLDVSVQ
     QSIVYAAAVL LAEHGLTPTP SRAEALARVL QSAVLSGVYV APGTYELLRW AKRNGILVGI
     VSNNWCYECV RLLLERDDLA HLVDTVVTSD IVGFCKPHTK IYEAAMQLLR ADPAKTAFID
     DYEPNVEGAR RAGIGLAIHH DGKPLDHYIP VLERFYSSR
//
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