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Database: UniProt
Entry: G4F1K6_9GAMM
LinkDB: G4F1K6_9GAMM
Original site: G4F1K6_9GAMM 
ID   G4F1K6_9GAMM            Unreviewed;       653 AA.
AC   G4F1K6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Xylanase/chitin deacetylase {ECO:0000313|EMBL:EHA17359.1};
GN   ORFNames=HAL1_01242 {ECO:0000313|EMBL:EHA17359.1};
OS   Halomonas sp. HAL1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA17359.1, ECO:0000313|Proteomes:UP000005692};
RN   [1] {ECO:0000313|EMBL:EHA17359.1, ECO:0000313|Proteomes:UP000005692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX   PubMed=22156396; DOI=10.1128/JB.06359-11;
RA   Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA   Wang G., Rensing C.;
RT   "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT   Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL   J. Bacteriol. 194:199-200(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA17359.1}.
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DR   EMBL; AGIB01000006; EHA17359.1; -; Genomic_DNA.
DR   RefSeq; WP_008956185.1; NZ_CP130610.1.
DR   AlphaFoldDB; G4F1K6; -.
DR   PATRIC; fig|550984.5.peg.246; -.
DR   Proteomes; UP000005692; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0043708; P:cell adhesion involved in biofilm formation; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 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   InterPro; IPR023854; PGA_deacetylase_PgaB.
DR   InterPro; IPR032772; PGA_deacetylase_PgaB_C.
DR   NCBIfam; TIGR03938; deacetyl_PgaB; 1.
DR   PANTHER; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF7; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR   Pfam; PF14883; GHL13; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000313|EMBL:EHA17359.1};
KW   Glycosidase {ECO:0000313|EMBL:EHA17359.1};
KW   Hydrolase {ECO:0000313|EMBL:EHA17359.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:EHA17359.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:EHA17359.1}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..653
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003462985"
FT   DOMAIN          93..338
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   653 AA;  75166 MW;  2197BBC1F4D09C8B CRC64;
     MTLWRVIMMS AVLLVIVNIQ QAQAARSADD YVVISYHDVV DSTVTPDLDI YSQTITRGRL
     VEHFNLIALG GYQPVSLQQI IDAKAGGQPL PEKAVLLTFD DGYRSFYDIV FPLLKLYDFP
     AVQAVVGSWL DVPAGGQVPY GKINLPRERF LSWEQVKTLD ESPLVEIASH TYNLHYGAVG
     NPMGNEQAAA VTSIWNAGNG YESEADYIER IRNDMARTQQ QFQEKIGKGP RVMVWPYGAY
     SEATLNIASE YGMKYTFSLL GEPNRLNDSM RSMNRFLIDQ ETTLETIEEI LSNRLWETEE
     QRIVHVDLDY VYDPDPIQQE QNLDRLIERI SRYGVSTVYL QAYSDPDGDG VADELYFPNR
     HLPVRADLFN RVAWQLKKRA NVKVYAWMPV LSFDLGDGYQ YVTDVRTGNE SPDHYRRLSP
     YVIENRNTIR EIYLDLGRLT KFDGLLFHDD AFFTDFEDAN PEALDAYELA SLPRDINAIR
     NDENLMATWA RFKGEHLTDF TLELEKAANY YRQSDNKVFT TSRNLYAVTV MEPRSKRWFA
     QDMQNFASAY DFVAVMAMPY MEKAENPNQW LRSLAQRSLE QVSADQLVFE LQAQDWNTQT
     PIPSAEIAQW VRILREEGIK NIGYYPDDFL QNHPDINVMR PVFSIGRRFR AIP
//
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