ID A0A0M9YB00_9ACTN Unreviewed; 693 AA.
AC A0A0M9YB00;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KOU38202.1};
GN ORFNames=ADK54_28950 {ECO:0000313|EMBL:KOU38202.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU38202.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOU38202.1}.
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DR EMBL; LGDD01000307; KOU38202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9YB00; -.
DR PATRIC; fig|1415557.3.peg.6362; -.
DR OrthoDB; 9770043at2; -.
DR Proteomes; UP000037774; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04082; CBM35_pectate_lyase-like; 1.
DR CDD; cd00063; FN3; 2.
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; IPR005084; CMB_fam6.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07995; GSDH; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50853; FN3; 2.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..693
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038704745"
FT DOMAIN 42..167
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 179..266
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 274..365
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 72383 MW; 1B2238D57A0F82F1 CRC64;
MRLATPPRPA RGRARKAAAA AVLLLCAGLV QAAPQPASAA STRYEAESGT RSTGSTVDTN
HKNYSGTGFV NSNNAVGAYV EVTVNVAAAG NATIDIRYAN GTGANRPADV SVNGAVVSVA
RAFDATANWD TWADSTLTVA VKAGSNKIRL ASTTADGLAN IDYVDFSGAS GGDTQAPTRP
GTPTCSAVTE SALTLSWGAS TDNVGVAKYD VYEHGNKINE VDGTLTSDHL TGLTPNTTYN
LTVLARDAAG NVSQASPAID CTTPPSTDTN PPTKPGTLTS SHVTANSVDL NWGASTDDKG
VTSYEVRSGD NVYKAVTGNP PGTSTTLTGL ACDSPYSLTV VAKDAGGNVS PASNAVSFTT
ATCQTDGGVP SSITTLSIDW TIPWGTYWMP DNSSALVTER DSFKVYKVTP NGTKTQVGSV
PNAVTTDGEG GLLGVAVDPK WATNHYVYFM HTAAEGNRVV RMTYNGSALS NYTVLLQGIK
KNRYHNGGRL AFGPDGYLYA STGEAQTPDL AQDKNSLNGK ILRMTTDGKP APGNPFNNYV
YSYGHRNPQG LAFDRNGRLW EAEFGDSKKD ELNLIKPGAN YGWPTCEGPC STAGMTNPKA
SWPTGQASPS GIAIVRNVVY MAALKGERLW RIPITGDTEN VGTPTAYYVG SYGRLRTVTK
VPGEDAFWLS TTNGDNNGTG GAGSDKIFKV LVK
//