ID J9SC11_9ACTN Unreviewed; 433 AA.
AC J9SC11;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Phosphodiesterase / alkaline phosphatase D {ECO:0000313|EMBL:AFR48254.1};
GN ORFNames=KTR9_1614 {ECO:0000313|EMBL:AFR48254.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48254.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR48254.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR48254.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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DR EMBL; CP002907; AFR48254.1; -; Genomic_DNA.
DR AlphaFoldDB; J9SC11; -.
DR STRING; 337191.KTR9_1614; -.
DR KEGG; gor:KTR9_1614; -.
DR PATRIC; fig|337191.3.peg.1878; -.
DR eggNOG; COG3540; Bacteria.
DR HOGENOM; CLU_015982_2_1_11; -.
DR Proteomes; UP000003281; 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; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
FT DOMAIN 1..51
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 64..402
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 47689 MW; 529D49EC43970FB7 CRC64;
MTRIVRRGTV HATPEWGHSV HVDVRGLAPA ADHFYRFRAL GEISTVGRTR TAPAPSAHVD
TLTLAVATCQ NWADGYYQAY ADLAAHAPDV VLHLGDYIYE KPIPAQGGAR TTAALPLSST
REAVDLDDYR ERYALYKSDP DLQLAHAMAP FVITFDDHEV DNNWAAAVPE DDTPPVPFAL
RRARALRAWW ENSPVRVTAR PNGTVVRAHR RLGFGDLVDL TLLDTRSHRS DQANGDNDTG
QNQHTADPSR TILGAEQERW LLDGFASSRH RWDVLAQQVP MADLARTVGS TRAVSMDGWS
GYEASRARIL DGATDRGVRN LVSLAGDIHR SVVADLRTSY TDDSAVRGVE LAATSITSGG
DGEDSDDGDR RLKEASPHVR FGNSQRGYLL NRIHSDRWEA EFRVTPSVRS PRGTLHRRAL
ITIPDSTAEV DVV
//
