ID A0A1I1BGN0_9ACTN Unreviewed; 2280 AA.
AC A0A1I1BGN0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glucose/arabinose dehydrogenase, beta-propeller fold {ECO:0000313|EMBL:SFB49297.1};
GN ORFNames=SAMN05192575_1212 {ECO:0000313|EMBL:SFB49297.1};
OS Nocardioides alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=748909 {ECO:0000313|EMBL:SFB49297.1, ECO:0000313|Proteomes:UP000199113};
RN [1] {ECO:0000313|EMBL:SFB49297.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10697 {ECO:0000313|EMBL:SFB49297.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOKC01000021; SFB49297.1; -; Genomic_DNA.
DR STRING; 748909.SAMN05192575_1212; -.
DR OrthoDB; 6402258at2; -.
DR Proteomes; UP000199113; 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; 1.
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; 4.
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; 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; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF17851; GH43_C2; 2.
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; 3.
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; 3.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50093; PKD; 2.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2280
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039345254"
FT DOMAIN 767..851
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 964..1095
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1105..1188
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 38..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2280 AA; 238021 MW; CBF8D1E28B1AFAB8 CRC64;
MNRIITRPSR RSRTLLGSTM AMLVALPLGA TLGMGTAASA AASGPDTPER TSTSTANTST
DKPAKAELPS TPLAEAVPWT VDPKAPAAAA AAGDPFKALV FSETAAFRHS NIDEATTAIQ
QLGAANNFTV TTSEDSSVFT DANLAQYEVV IFLSTTGDVL TTVEQAAFER YIQAGGGYAG
IHAASDTEYD WPWYGNLVGA YFNNHPNGTP TATVKVEDPA HASTAGLPKR WERTDEWYNF
RTPNNLTARN KLHVLASMDE TTYAPGTGAN GVEHPISWCQ DYDGGRSWYT GMGHTEANFT
DANFLKHILG GIQTAAGVVA SDCKATLQPS FEKVALDENT TNPMELTIAK DGRVFYIDRA
GAVKIILTNG SVVTAGTVPV YTGQEFGLLG IALDPNFATN GHVFLYFAPQ GTESIDRISR
FTVTGNTMSL ASEVKILDVP VQRNECCHAG GSMEFDQDGN LYLATGDNTN PFDSGGFNPI
DERAGRSAWD AQRTSANTND LNGKVLKIKP ALAGGYTIPA GNLFDEAADA TQKTRPEIYA
MGFRNPFRIG LDEQNNKLLV ADYGPDSGST SATRGPNGRV EWNILDQPGN YGWPYCVGNN
TPYNDYNFAS STAGATFNCA APVNDSPNNT GLTNLPPAKP AVIWQSNNAA TTGTPEIGAS
GAPMTSGTYK FDPNLVSDRK WPAYFDSKAI WADWNNSRLF TVQMNDGGTN YTDINRFLPN
LAMSRPHALQ FGPDGALYMI EWGSGFDGNN ANSGIYRIDY VEGERSPTAR ATTNKTSGPA
PLAVTFDGTT SIDGDSGTNA GLTYAWDFTN DGTVDATTPT ATYTYATAGN YTARLTVTST
NGKTGTTNID IVAGNSAPVV DLQLPLNGGF FEFGDTIKYT VSVTDPDGGT VDCTKVVVQP
GLGHDQHSHG YEQYTGCSGS FVLPGDAGHS GANVFGTVTA TYTDAGNGAA GPLTGVDGAV
LHTKKKEAEF YDQTGRTGSE TAGTPGVITQ TTTDTNTGLN ITGVETGDWF GWDVMNLTNI
TGVTMRAAST TGGTFAVRQG SPTGTTIGTL TVPATGGAQT WQDVTTTFTG ATTTSVPLYV
VATTGGVNVN WLQFNGRGVT DNTPPAVTIA ASKLTGSAPL PVAFTSTVTD ADNDTPVTYA
WNFGDTTTST EANPSKTYTT PGKYTVSLTV TDARGAKTTK TLEINVTVAE NICFSGRSDD
FLGTELDVTR WNRNVRVNQG LTVAGGSLNI PLTNSDLYQT TNTTPNIVLQ DLPAGAFEVT
TKVDLTGANK GYQQGGLIIY GDDNNYLKLV YSGRSTAAAG SKAANVIQFT KETNATASET
NSAALGAAFP DTVWLRMSST NGSSVTASYS SDGATWLPVT AANAARDLTG ITAPKVGLLA
LGSTTAGAAD NLTAKFDYFT LTPDDTAVPC ATPCQAEQFN GSALDAATWN DSVRLNSSLT
VADGTLNIPL TNSDLYQTTN TTPNVVLQDL PSGKFVVTTK VTLNATKGYQ QGGLIIYGDD
DNYIKLVYSG RSTAAAGSKA ANIIQFFKET NAVASETNGA ALGADFPDTV WLRLSSTDGN
AMTASYSSDG ATWLPVNAAN ATRDLTGITA PKVGLVALGA TTAGAADNLV AKFDYFTLGK
DDTCVPPAGP SDTTAPTTTL TIPAATGQAG WYTTRPSFTL AAADGAGGSG VASTEYRIAG
GAWTPYTAAV SVTGEGTRLV EYRSTDSAGN VEAIKSESVK VDTVTPTVSG AATGDTTKTV
TLTATDATSG IASIEHQIGD ATTWTTYSAP LTFDQPGTYV VRYRATDVAG NRSTGQLEVV
VPQPADTTDP EVDATVLGSY AGVLVDQAST GVSGKATMVS TDDGTTVELT LAGLDPTQDY
ESHLHVGTTC GGFAGHYRND PAGDGTPPNE LWPTNPGWVA GSGDARIEAA ADGTSFATAT
VPWAPRIEGG ILALHREGAI IGCVDLDLTG PGTVVLDATD NVDVTSLTYT VDGGAETEYD
GPFEITQPGE HVVAYTATDA AGNETIGELT VVVPEEPVVE PPVETAKPTV SISTAPAAAN
GRSNWFTSPV TITLAGAGGT GKVTVEYRIG NGAWTAYTTP FQVAADGVTL VQARATDEAG
KASAVATTTI KMDATAPVVT ISGIADKAKL DLAAVRIALV TAVDATSGVT ERIIRLDGEV
VSSPAQIDAL SLRSGKHSLE VTVTDEAGNQ TSRTITFKVV ASIGGAKKLV NRLDDENTIG
AKLGTKLKQE LKAVKRADRS GTEREARMAL KRFKKLASRV KDDEARRALK NLARTLKSEL
//