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Database: UniProt
Entry: A0A1H2JYE0_9ACTN
LinkDB: A0A1H2JYE0_9ACTN
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ID   A0A1H2JYE0_9ACTN        Unreviewed;      1922 AA.
AC   A0A1H2JYE0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glucose/arabinose dehydrogenase, beta-propeller fold {ECO:0000313|EMBL:SDU61457.1};
GN   ORFNames=SAMN04488563_3219 {ECO:0000313|EMBL:SDU61457.1};
OS   Jiangella alkaliphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC   Jiangella.
OX   NCBI_TaxID=419479 {ECO:0000313|EMBL:SDU61457.1, ECO:0000313|Proteomes:UP000182977};
RN   [1] {ECO:0000313|Proteomes:UP000182977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45079 {ECO:0000313|Proteomes:UP000182977};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629791; SDU61457.1; -; Genomic_DNA.
DR   STRING; 419479.SAMN04488563_3219; -.
DR   Proteomes; UP000182977; Chromosome i.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR009784; DUF1349.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR012938; Glc/Sorbosone_DH.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   InterPro; IPR029010; ThuA-like.
DR   PANTHER; PTHR40469:SF2; PROTEIN WITH GLUCOSE DEHYDROGENASE; 1.
DR   PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF07081; DUF1349; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF07995; GSDH; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF06283; ThuA; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00089; PKD; 2.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1922
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009277945"
FT   DOMAIN          729..812
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          925..1044
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   REGION          861..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1922 AA;  204283 MW;  18C3C6F46FB5DDC2 CRC64;
     MLVALRQRWS RLMAVALAAV LAIPLLTALP STAHEGEHGE EAHVLIFTKT TQFRHTEAIT
     QGVPVLQAAF EAAGITSEHT EDSSIFNDED LSHFDALIMF QASGDPWTAE EKAAMERYQQ
     AGGGIVAIHN SADMRGNYAW WDTLIGSLMP GHAATGSSPG LPGTVRIEDG VHPSTTHLPQ
     RWERADEWYN FSANVRGTAH VLATMDETTY DPGGNAQGYD HPISWCKPYD GGRAWVTAMG
     HFGAHYTQEP DFVQHILGGV QWAAGVAEGD CGGTVWDQYE KVPLDQNTSA PFAIDVAPDG
     RVFFTELVRG QIRVYDPATQ TTSTAITIPV YSGGEDGLLG IALDPDFETN GHLFVYHSKA
     SANDSDPANF ISTLSRYTVG ANSQIDPASE VVVLEVPARR LPDEPGHTGG GLAFGPDGNL
     FLSVGDDVNP HSEPSGGYAP LSERAGTFHD ARETSANTND LRGKLLRITP QPDGSYTIPE
     GNLFPEGTAQ TRPEIYAMGF RNPFRFSIDP ETGWVGLADY GPDNGSDSAT RGPAGMVEWN
     LIKEPGFYGW PLCIGPNEPY LDVDYTTNPV TVGAPFDCDN PVNDSVRNTG LTELPPVQEP
     EMYYGYDSSS VPGVIPAGGG LAPMGGPFYQ FDPELDSDTK FPEYYDGKPF FYEWAKNRLY
     SIDLNQETGD VEKVNPFLPP PNEQWMAPID SQFGPEGSMY VLDWGGGFGR DNPNSGLYRV
     DYVSGSRSPV AHATATPDSG QAPLAVQLDG SGSTDPEGEA LTYAWDYTND GTVDSTEAQA
     SFTYTENGVY NARLTVTDPH GKTGTTTVPI TVGNTRPEVT FDLPPDGAFF DFGDTVAWDV
     EVTDAEDAEI ADEDVIIQPA LGHDEHPHPA DPLSGRTGQV QTALGGGHSE DMNVFYILNA
     RYTDGGGAGG IPALAGEDTS LLFPRQREAE FHDDAEGVTT GPSRDVEGHG TAIAGADGAW
     ASFDPVNLLN VDALVLRASS SAGGPIELRR DAPDGPLLGT GQVPATGSGY ADVAVEVDDP
     GESFTLYAVF PGAGERRLNF IEADGKGAAT TSKPKVAITA PTPADELELG EVQVTADASD
     AENTITQVEF FVGDDSIGVD TEAPYEATWT VTEEQRYQLT AVATNNLGAS STSRIVQVEI
     GDLFGDWLTY SHASAAGTFD RPDNNTWVIE SGGGNMWQGT DEYSAVYLPG AAGATGDQWT
     ATAKVVSQTN SNASAKAGLI VRNDVTQPGV SPGYAAMAMR AGLSFEWLRD SDGNGQLDAS
     TSAGQNGYPA WVRIVRDGDL YTSYWSRDGE TFTQVGEPVA LPGATDVQDI GLAVTAHSGS
     ARTAAVFTDF VLEDGLPGEG PDPEEPPVCL ITGTDQFDGD ALNETRWTTV RGADGLPASV
     ADGGLVLPVT NGDINEAVAG PISYVGQPTR DGAWTVETEV SVAHTREWQH AGLLMHGTDD
     DYVKLAFTRT NSGSRILEFQ TEAGGTRTWH ANVTLPADFP STAHLRLASD GEQVTASYSA
     DGETWTALSG AAALVEDSTI GLMAAGDTAP HAVNAVFDHF TITPDVEDDG QREPTDEFDG
     SAIDGCRWDS VVRYDSTAAS VADGQLRIQT QPGDINGAAN ENPRNFILQE VPEGEDWTIE
     TRVTPTMLHQ WQLAGLMVYG DDDNYVKFDV VANNTAGAAT NLRAELVSEK GGQFGNGGNR
     NIDIPETSES GWYYLRLTRS GDTYAAEISD GGVNWTSLGD PVTNDAELTS FGLMAIGPQQ
     TQPVTVAFDY FRVTTDQPDT TPPAITVEGV ADGGGYDLAT ALELSATATD DVSRDVVVLL
     TLDGEAVENP SAVTPELGAH TLVAIATDEA GNAAETTVAF EVVATFDGAQ ALVQRYRADG
     TVQRSVATQL NTHLANAERL AGQGTSGAAT SLDRYEALAE GVTDETARGW LLAYADALRA
     QL
//
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