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Database: UniProt
Entry: D2S3E1_HALTV
LinkDB: D2S3E1_HALTV
Original site: D2S3E1_HALTV 
ID   D2S3E1_HALTV            Unreviewed;       323 AA.
AC   D2S3E1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:ADB63888.1};
GN   OrderedLocusNames=Htur_5257 {ECO:0000313|EMBL:ADB63888.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG   Plasmid pHTUR04 {ECO:0000313|EMBL:ADB63888.1,
OG   ECO:0000313|Proteomes:UP000001903}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63888.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB63888.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RC   PLASMID=pHTUR04 {ECO:0000313|EMBL:ADB63888.1,
RC   ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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DR   EMBL; CP001864; ADB63888.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2S3E1; -.
DR   KEGG; htu:Htur_5257; -.
DR   eggNOG; arCOG09177; Archaea.
DR   HOGENOM; CLU_071509_0_0_2; -.
DR   Proteomes; UP000001903; Plasmid pHTUR04.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10929; CE4_u5; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:ADB63888.1}.
FT   DOMAIN          38..157
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|Pfam:PF01522"
FT   REGION          304..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  35806 MW;  F1FAC8C988424AD4 CRC64;
     MVGAVGSVVV SLDAELGWGF HDLPEPPADR VESGRRGWSV MLELLDEFDV PATWAVVGHL
     MLESCDGVHE DHPAPPGWFD RERGAWADRA DLRFGPDLVE GVLEADADHE LASHTFSHVL
     FGDPRTDREL AAAELDRATD IAAEWGESID SFVYPRNDVG HRDVLAEYDV SAYRGRSPTR
     DGVRGVFDST VRDQSLVTTP RTDEHGLVNV PASLFLFGFE GPARTVAESI WTDPMLELAR
     RGIDEAVRSD GVFHMWLHPN NLTSERDDQR MRSILSYLER RRSETDLTVE TMGDVARRVR
     RASETGIDGA TDGVDGQATV RSN
//
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