ID A0A2K8P9A8_STRLA Unreviewed; 799 AA.
AC A0A2K8P9A8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:ATZ23306.1, ECO:0000313|EMBL:QUQ53137.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:ATZ23306.1, ECO:0000313|EMBL:QUQ53137.1};
GN ORFNames=SLAV_07005 {ECO:0000313|EMBL:ATZ23306.1}, SLLC_05020
GN {ECO:0000313|EMBL:QUQ53137.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ23306.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ23306.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ23306.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ53137.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ53137.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP024985; ATZ23306.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ53137.1; -; Genomic_DNA.
DR RefSeq; WP_030224549.1; NZ_JOEW01000001.1.
DR AlphaFoldDB; A0A2K8P9A8; -.
DR GeneID; 82163448; -.
DR KEGG; slx:SLAV_07005; -.
DR OrthoDB; 9816160at2; -.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; Chromosome.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ATZ23306.1};
KW Hydrolase {ECO:0000313|EMBL:ATZ23306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231791};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..263
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 316..711
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT ACT_SITE 492
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 353..354
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 612..613
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 799 AA; 88704 MW; 6B63D0351D2E9AA9 CRC64;
MTTAWHWEYD RYDPKTERLV EALCTLGNGR FATRGSAPES VADEIHYPDT YLAGCYDRLD
STVGGRTVSN EDMVRLPDWT ALRYRCLPEG APPGDWLTPD HPSLRHSHVS LDLRAGTLTR
RMLFHDAEGR RLGVTHTRLV HMGDPNLAAQ NTVFRAYGWG GGIEVESVLD GDVTNAGVER
YRALAGRHLV VHRTGVEAEG AAWLSCTTST SRVVIGLAVR TATHPLAQVG RACTATTATQ
TFVLPIRRAA PVVVVKTAAL CTSLDRPPAD PLRRSIDCAV HAPDFSSLLT SHRASWQCLW
SDGELKVPGE TGEVLRLHAF HVLQTLSPHT AELDAGVPAR GLHGEAYRGH VFWDELFVLP
YLALHLPETA RALLAYRHRR LPAALEAARR AGANGAMFPW QSGSSGTEET QRLHLNPRSG
RWLPDHSHLQ HHVGSAIAWN VWRYGLATGD AGFMHGPGAE LLLHIARFWA DSATWDTGLS
RYRIRGVVGP DEYHDAYPDA AAPGIDDNAY TNVTAAWVLA RALDLYGELP AARRAELLTR
LGIGPDDLTL WEDVSRRLYV PFHRDVISQF HGYGDLDELD WDGYRSRYHD IRRLDRILEA
EGDTPNRYQA SKQADTLMLG HLFRPSELEQ LFLRLGCRFD DGLWRRTVEY YLRRTCHGST
LSSLVHGWIL AREQGPDAWR YCQEALLGDI TDVRGGTTGE GIHLGAMGGT LDLVERGIVG
LEPHADGLHI DPVRLSEVPG CSFSISYLGH RDIHVRFRPG RLGISVPPSL LGPVPLVLPG
DRHERISAGQ ERWFRLPKG
//
