ID F3ZAA5_9ACTN Unreviewed; 642 AA.
AC F3ZAA5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Putative xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:EGJ74953.1};
GN ORFNames=STTU_2164 {ECO:0000313|EMBL:EGJ74953.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ74953.1};
RN [1] {ECO:0000313|EMBL:EGJ74953.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ74953.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family.
CC {ECO:0000256|ARBA:ARBA00008875}.
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DR EMBL; CM001165; EGJ74953.1; -; Genomic_DNA.
DR RefSeq; WP_007822501.1; NZ_CM001165.1.
DR AlphaFoldDB; F3ZAA5; -.
DR HOGENOM; CLU_028597_0_0_11; -.
DR Proteomes; UP000003955; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR049166; GH39_cat.
DR InterPro; IPR000514; Glyco_hydro_39.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR12631; ALPHA-L-IDURONIDASE; 1.
DR PANTHER; PTHR12631:SF10; GLYCO_HYDRO_42 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01229; Glyco_hydro_39; 1.
DR PRINTS; PR00745; GLHYDRLASE39.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 159..606
FT /note="Glycosyl hydrolases family 39 N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01229"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600514-1"
SQ SEQUENCE 642 AA; 68740 MW; 40A96B3ED2E03B63 CRC64;
MPEKPAAPAH PAAPDAPAAA PAAPTAAPEK SAARSDWEQR IGKPSDTRLT GTAAVAAPAG
LRAEEGTGLV RLDWRPVAGA LGYLVHRADS PEGPFTPLDH LGGDVLAVPH PPYADTLVEP
GRAYHYKVAS WTDDGAGPLG AETVTATPKA PGEAPAAVEV AVDAAAPTSP LPRVWNRIIG
AEHLSLLLWD KPGPGGSDTA AEYHEALGKV RDELGVRAVR AHGTFLPETV SVRPDGSFDF
SGLDEVYDRF LATGLKPVVE LSFMPEELAK DPGYTVFDYK ALVSTPTSWE RWGELCHALV
VHLQERYGRD EVAGWEFEVW NEANLEVFWN GTQDDYHLLY AYAVRAVKAA DPRIRVGGPS
SAAAGWVGAL LEYCRAENLP VDFVSTHTYG NAPLDFRPLT RAYAEATGRP EPEILWTEWG
VTPTHFHPVS DSVFSAPFVL RGMKSALAST DALAYWVATD QFEELGWPPK LFHGGFGLLT
VGNLRKPRYW ALWLLNQLAG DRAPVAVSGD GADATVEALA TRAEDGSAVD VLVWNGTLDQ
SKVAGAAALG RSTTVRVTGL EPGARYAVSA YRVDEAHGNI QAVWEEIGGG DWPDAPQWAK
LREADRLPAE PLAPVLADAA GTVRVEVELP MPGIRLLGLR RA
//