ID A0A0K1K4B2_9BURK Unreviewed; 838 AA.
AC A0A0K1K4B2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphodiesterase {ECO:0000313|EMBL:AKU24043.1};
GN ORFNames=ACZ75_23915 {ECO:0000313|EMBL:AKU24043.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU24043.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU24043.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU24043.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012201; AKU24043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1K4B2; -.
DR STRING; 1678028.ACZ75_23915; -.
DR KEGG; mnr:ACZ75_23915; -.
DR PATRIC; fig|1678028.3.peg.4856; -.
DR OrthoDB; 327733at2; -.
DR Proteomes; UP000056897; Chromosome.
DR CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR InterPro; IPR032093; PhoD_N.
DR PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR Pfam; PF09423; PhoD; 2.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000056897}.
FT DOMAIN 52..158
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 171..446
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT DOMAIN 597..673
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 26..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 87047 MW; FB60A7505DC2B95F CRC64;
MDRRQFMKLG GFITVSVASA GLAGCGGSSN SGDSAPGGLP PATGGDWKFP QSVASGDPRP
DSILLWTRAV PAASDGVAAV GGKAEVTLRL LLTASDNSAL LGSNAALGGS MLSDVRLPLN
PEFDNTIRHK VTGLQPGQTY YYQFVAGDVR SNVGRCKTAP AATADVDQLQ FAYLTCQDWS
INHWGALGHI AANEKLDFIV HLGDYIYETV GESFQTGLVE SRHDALKLPD GTFKNGSAGA
KYASTLADYR YLYKKYRSDT RLQAVHERFP FIAVWDDHEF TDDAWQDAQT YEGSLAADGS
HVRQPQRRRS ANQAWFEYMP ADVSLDTAAS GFQNIKIYRD FQFGKLAQLV MTDQRLYRAD
HVIPEATPNP ATGKALGSIG TRYMVAQDVF NAAEAQKMAA AGAAGDALAA TTMLGATQRD
WWKSTMKSAS ATWKLWGNEV SLLRMGLSGV DAIATLLALK ALPDLAGKIG STAAQAGGNV
AVAGAIVGAV TAGAAPDKAQ AAAGAIATAA AANGDTVART TAAMGAGLSQ IQAGLAVLAF
GMAQSVAAGG ASAQATAAAQ AIAVGYIKPD VQAKKAESPF VAAAGLQAAL APYFRRFLLN
CDQWDGYNAE RKALMSHLKT NAIGNVVALT GDIHAFFAGT VSDDYDAAGG GTPVMVDLVS
AGISSDSFFS YLRDASAALG ELGALVAYPL TLPVPELGAV SISVNLLDYT MGKAAPTLDT
LLEQVKVQLR GALAAKGVPE GQLDTVTLGL LAGLKANSGF STTLLGLAQQ LAGLNSNPWL
KHLNTDAQGY TVVTLTPGKL VAQFKQVNKL VGATAPANVI ARITTATVAA GTPAVTIS
//
