ID A0A660L0L3_9ACTN Unreviewed; 1785 AA.
AC A0A660L0L3;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glucose/arabinose dehydrogenase {ECO:0000313|EMBL:RKQ84800.1};
GN ORFNames=C8N24_6430 {ECO:0000313|EMBL:RKQ84800.1};
OS Solirubrobacter pauli.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Solirubrobacteraceae; Solirubrobacter.
OX NCBI_TaxID=166793 {ECO:0000313|EMBL:RKQ84800.1, ECO:0000313|Proteomes:UP000278962};
RN [1] {ECO:0000313|EMBL:RKQ84800.1, ECO:0000313|Proteomes:UP000278962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14954 {ECO:0000313|EMBL:RKQ84800.1,
RC ECO:0000313|Proteomes:UP000278962};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKQ84800.1}.
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DR EMBL; RBIL01000003; RKQ84800.1; -; Genomic_DNA.
DR OrthoDB; 5522149at2; -.
DR Proteomes; UP000278962; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 2.60.120.200; -; 2.
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; 3.
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; IPR014756; Ig_E-set.
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; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 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; PF00801; PKD; 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; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50093; PKD; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Reference proteome {ECO:0000313|Proteomes:UP000278962};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1785
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039612931"
FT DOMAIN 726..808
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 923..1052
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1062..1149
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 403..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1785 AA; 188505 MW; 9AC9A01B5A9D877B CRC64;
MKLRWKAVAL AAAVLGASAA PAAAQTPRFD VLVFSKTTGF RHSDAIDAGK TGIQALGTAN
NFNVTITEDA TQFTDANLRP YEVVVMLHPD GEGILNAAQR TAFERWYQRG KGLVGIHAAA
NADRDWDWMA DARGGSLFNN HPAIQQATVK ITEPDHPATQ GIPADWVRTD EWYNFTKEPA
GVKVLAKLDE STYNEEDGSA EADDHPIVWC SNFDRGRSFY TALGHAGTAW DEANYRKHIL
GAIEWAAGTA PGDCGAPRDG IPTDASFDKV TLDDNTENPM EIAIGPGGNV YYVELAGKVK
LYNAATRSVR TVGTIPVHRG NENGLLGIAL DPNFATNKWL YLFYSAPSPE EQHVSRFTLN
EAGNVDLTSE KVLLKIPHQR IVCCHSAGSM AFGPGGLLHI STGDDTEHSQ SQGYNPIDDD
VIRNNPGDNP DADRAYDARR TSGNTNDLRG KILRIKPEPD GTYSIPAGNL FPPFQSDATK
TRPEIYTMGH RNPFRIAVDQ QTGWVYNGEV GPDANSENAN RGSRGYDELN QIRQAGNMGW
PYCIADNKAY RDWTFPSGPA GETFDCAGGP NNTSNYNTGL AKTPPATGAL LWWPYSPYPS
GFPWASGPTA IPTGSGRTAI AGPTYHFDAG SQADTKLPAY YDKKVFFADW SRDWIATLTL
DAQGKPAEVR RFMPGADFRH PQDIEMGPDG TLYVLEWGRD FNYAGSGINP DSGLYRIDYV
KGSRTPVAKA AVDKDSGALP LVATFSSAGS EDPDGDTLTY EWDFGDGSAK ATAANPTHTF
TTGGTYTVKL TVTDTSGKSG TSTVLVTVGN TRPTVALDIP QGGVYGWGDS IAYKVTVTDP
EDGTIDCSKV VVSPGIFHDE GGNAHVHPGV NKTGCEGTIQ VEQESGHEKS ANIALVLTAT
YLDNGAPNSQ PLEGATTRRL NPKEIQAEHY SGQNGTTAVD NASADGGRRV SSLDPGDSFF
FEPVSLKGVQ RVSFRYASTG AGGLAELRLD SPTGPVVGTA DLTASGGANV YKTGTATITA
PDDASHKLYV VAAARTGGPT TALYDIDSLT FSGKGVAANA APEVSISADA VSGVAPFPVT
FTGNVLDPEG GALTYAWDFD SNGTTDATTK DATHIYTAVG SYTATLTATD AGGKHQQATI
RIDATTAVAS CPGDDDFLGT SLNTGKWSVV REDPTAMNVS GGSLNITSQN FDIHGGGTGL
RNIVTQPLPT SGAWTATIKA NWDPTTNYNN AGLMVYGDDA NFIKAGMVWS GGRKFEAFKE
LNNTATALGS ATATLPGTFP TTWYLRLTSN GTTIQPAYSA DGITWTNYGA TTNLTGITAP
RIGVYATSAS AVNRELKVDW FKLTTPETPA DEFDGAALNL CRWTDIVRHE PGGYTVADGK
LTLPAAHGDF FANGANNNPN MLLQRAPTGP WTMETRLTFD PNENYEQAGL LVYGDDGNYV
KADYVYSGGR VLEFLNETNN VAAGFDGAAN INSRPTTVNL RIVSDGTTLR AYYRFDGDAA
WTTFGSPTAL SIAGANPKIG IYANDSNATV TTRDNAVFEY FRITAGVPDA TAPTSAATTA
GTGPVTVTVT GADESGGSGI DKLEYRLDGG AWTAYTEPVV VSAVGAHTLE HRATDKAGNV
STVGSVTFTI APPTTGESVT KDVDLSGSVP GTLALTIGTP PAFGTFMPGV TAEYNASAQL
QITSTAADAK LTVSDPSAVH TGKLVNGTFG LPQPVQVKAT SARGGTGAFA PVGTTSAPTT
LLTYSGPVGK DTATIDFKQS IAETDDLRRG TYAKALTFTL STTTP
//