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
//