ID A0A221W341_9PSEU Unreviewed; 1160 AA.
AC A0A221W341;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=PKD repeat protein/glucose/arabinose dehydrogenase {ECO:0000313|EMBL:MBB5919036.1};
DE SubName: Full=Quinoprotein glucose dehydrogenase B {ECO:0000313|EMBL:ASO20250.1};
DE EC=1.1.5.2 {ECO:0000313|EMBL:ASO20250.1};
GN Name=gdhB2 {ECO:0000313|EMBL:ASO20250.1};
GN ORFNames=AHOG_13035 {ECO:0000313|EMBL:ASO20250.1}, FHR81_000065
GN {ECO:0000313|EMBL:MBB5919036.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO20250.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO20250.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO20250.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5919036.1, ECO:0000313|Proteomes:UP000541573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8639 {ECO:0000313|EMBL:MBB5919036.1,
RC ECO:0000313|Proteomes:UP000541573};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022521; ASO20250.1; -; Genomic_DNA.
DR EMBL; JACHJM010000001; MBB5919036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221W341; -.
DR KEGG; ahg:AHOG_13035; -.
DR OrthoDB; 8217716at2; -.
DR Proteomes; UP000204221; Chromosome.
DR Proteomes; UP000541573; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008876; F:quinoprotein glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 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; 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; IPR008979; Galactose-bd-like_sf.
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; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF18911; PKD_4; 2.
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; 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 Oxidoreductase {ECO:0000313|EMBL:ASO20250.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000204221}.
FT DOMAIN 737..806
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 934..1067
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1078..1160
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 1160 AA; 124546 MW; E0920685D19679EF CRC64;
MRHPTRPRQI RGNRFAAALG GLFAMLLVVT TGLAATPAAG ATEARFSVLV FSKWTNFYHD
SIPAGIAAIE ELGAENDFDV TATDDAAAFT DENLARFDAI VFNNTNSTPE SGDLLDADQR
AAFQRYVQGG GGWAGLHAAS ASERDWDWYE GLVGAIFDHH PAIQPGRVKV LDRAHPSTEG
LPELWERTEE WYNWTANPTG NVHTLAQIKV RDGIEGLDEG VDHPFSWCQN YDGGRSWFTA
GGHASEDFSD ELFLGHLLGG IEWAAGAAEG DCSATRTGSF QRIPLVTEGL ADPFELAVAP
DRRVFYIERT GALKIVDQET LSVTTALDFE YTSEMTSQSD GLLGLTLDPA FEENGFLYLL
YSDKEENRLN VSRFTVDGDR VDEASEARLL EIPTFRGEGR ANSHMAGSLA MDDGGDLYIA
TGDNTDPFAS DGFSPIDERE GRRAWDAQAT SSNTDDLRGK ILRITPQADG GYTIPEGNLF
PEGTELTRPE IYVMGMRNPF RITVDSASGA LLVGDYGPDA RAADPDRGPE GTVEFDRITE
ASNRGWPYCT GDNTPFNDYD FATGTSGEPF DCTALVNDSP NNTGLTELPP ADPAWVHYAY
SESAEFPELG TGGGGPMAGP VYAYDEDNPL ITKFPEYFDG KWFTYELTRQ WFKTMSVHET
DQEFTDPRFE PTRAGDLLSI NGVFEDLEWV QPFEAEFGPD GSLYVIDFGE GSGTGRGGSN
EGSGIYRIDY VAEGRIPTAR VSASPDSGQG PLEVTFSSEG SGVGAGESVV YEWDFDGDGS
VDSTERNPTH VYPDDGQYSA RLTVTDPETE LAGVAVTTIT VGNTRPEVAI TLPAHGGLFD
FGDTIPFTVE VTDAEDAEID CSKVVVQSQL GHDDHLHPMD NVTGCQGDIT TDQGDSHGPG
QNLYAALSAQ YQDGGGVNGV PPLVGSAHAT LEPKRKEAEH FEDTGGENGG VEALARDDSS
AGHRIGEIEH GDWVAYDPIN LTGIDSVTLG VGSAGIGGTV EFRADGPDGE LLGSVDVENT
GGWGAVISPT VPLADPGGPV TLYLVFDNPE WTPDGHDLMS VDWLHFNGQG VTKEEISATV
VPTATPAAGT APLTVEFSAE VTVPEGREIV DHHWEFGDNQ YVHGETASHE YTRGGPFTAR
LTVTDDAGVR TSATVAVSVD
//
