ID E2PY22_STRCL Unreviewed; 1270 AA.
AC E2PY22;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:EFG10198.1};
GN ORFNames=SCLAV_5125 {ECO:0000313|EMBL:EFG10198.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG10198.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG10198.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
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DR EMBL; CM000913; EFG10198.1; -; Genomic_DNA.
DR AlphaFoldDB; E2PY22; -.
DR STRING; 1901.BB341_03365; -.
DR KEGG; sclf:BB341_03365; -.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG3828; Bacteria.
DR OrthoDB; 6402258at2; -.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 1.
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; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
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; PF06439; 3keto-disac_hyd; 1.
DR Pfam; PF03422; CBM_6; 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; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
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 Hydrolase {ECO:0000313|EMBL:EFG10198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT DOMAIN 538..619
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 731..856
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 136010 MW; 8060670D3F8E1746 CRC64;
MHPPFRKTPF GTAPRRRTPS GTGPTGGAPL SGAPLEKTPF GKAPFGGTRF RAALALVTSA
LLTAGTLTLA PAATAAVPPP PAPSQEDFQQ VTLAKGEAET GEPMSLAVLP DRSVLHTSRD
GDLRMTDSAG DTRVVGSLPV YTHDEEGLQG IGVDPGFERN RFLYLYYAPP LDTPPGDAPD
QGTPADFAAY EGVNRLSRFV LRPDGTLDNA SEKKIIDVPA TRGICCHVGG DIDFDAQGNL
YLSTGDDSNP FASDGYTPID DRPGRNPAYD ARRTSGNTND LRGKILRITV GAGGGYTVPS
GNLFAPGTPD TRPEIYAMGL RNPFRFSVDQ KTGHLYAGEY GPDAGAPDPQ RGPSGKVGFH
KITGPGNFGW PFCGTAGEPY VDHDFATGTS GAAFDCAAPR NDSRHNTGRT ELPPTRQAWI
PYDGNSVPEF GTGSESPMGG PVYRYDPDNP SPVKFPEAYD GDFFAGEFGR RWIRRVEHSP
DGSAGTINTF PWTGTQVMDM AFGPDGALYV LDYGTAWFGG DHNSALYRIE NATGGRSPVA
EASARRTSGT APLRVAFSSA GTTDADGDPL TYRWTFGDGA TSTAPDPTHV YRTNGTHTAT
LTVTDPTGRT GSASLRIVVG NTAPTVTLKK PALGTLFRFG DEIPFEVTVT DPEDGPVDCA
KVKVSYILGH DSHGHPLTTA QGCTGTIKTS SDGGHDPNAN IFGVLDAEYT DGGGGGQAPL
TTHDQAQLQP RHRQAEHHGA AHGITVYDKP TANGGKTVGD IHDGDWISFT PYRLTGATEL
TARISSGGSG GFLEVRTGAP NGRILGSTPV PVTGGWETFQ DVDIPLRAAP GRTTELFLVF
KGGDGALFDL DDFEITDSPP DRTAKRVLVF TRTEGYRHDS IPAGTAALRE LGRSSNITVD
TTETAAQFTT ANLARYDAVV FLSTTGDVLD TPQQHALEQY IRTGGGFVGI HAAADTEYDW
PFYGGLVGAR FSSHPHIQGA TVRVEDREHP ATRHLGPAWQ RTDEWYNYTA NPRPRVRVLA
TLDEATYEGG DMKGDHPIAW CQTYQGGRSF YTGGGHTPES YAEPAFRNHL LGGLRYATGQ
ARADCTPRTG ERPLFNGKTL DGWKQAGPGR FTVTDGELRT HGGMGLLWYQ AKEFTSYRLT
LDWKVDGDDN SGIFIGFPAS DDPWSAVTRG HEIQIDASDA PDRTTGAIYG FRSADLTARD
RVLRPPGQWN TYEITVRGER VQVFLNGTKI NDYTNTDPAR SLQDGHIGLQ NHGAADQVSF
RDITLRELPT
//
