ID A0A0U3JZF2_STRGL Unreviewed; 783 AA.
AC A0A0U3JZF2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:ALU92253.1};
GN ORFNames=WQO_02075 {ECO:0000313|EMBL:ALU92253.1};
OS Streptomyces globisporus C-1027.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172567 {ECO:0000313|EMBL:ALU92253.1, ECO:0000313|Proteomes:UP000064183};
RN [1] {ECO:0000313|EMBL:ALU92253.1, ECO:0000313|Proteomes:UP000064183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-1027 {ECO:0000313|EMBL:ALU92253.1,
RC ECO:0000313|Proteomes:UP000064183};
RX PubMed=22815456; DOI=10.1128/JB.00797-12;
RA Wang L., Wang S., He Q., Yu T., Li Q., Hong B.;
RT "Draft genome sequence of Streptomyces globisporus C-1027, which produces
RT an antitumor antibiotic consisting of a nine-membered enediyne with a
RT chromoprotein.";
RL J. Bacteriol. 194:4144-4144(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP013738; ALU92253.1; -; Genomic_DNA.
DR RefSeq; WP_032748696.1; NZ_CP013738.1.
DR AlphaFoldDB; A0A0U3JZF2; -.
DR STRING; 1172567.WQO_02075; -.
DR KEGG; sgb:WQO_02075; -.
DR Proteomes; UP000064183; Chromosome.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ALU92253.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..783
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006840640"
FT DOMAIN 123..198
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 241..334
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 377..489
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 638..777
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT REGION 42..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 84944 MW; 290947CD44AEE4EE CRC64;
MRPAPAPRRR TWWRRLTATT GLLALVATAL VGTGTAPAAA APAAWEPKPA PMTTPWTDSV
PVDKPLPEYP RPQLTRPDWT NLNGIWDFAV TGRDAGQPAT FPEQIRVPFV AESALSGIQR
RITENDKLWY KRTFTVPANW NNRRVKLHFG ASDWQTTVWV NGTQVGAHKG GFDSFAYDIT
PQLNGGTNTV VVSVYDPSQT GGQAVGKQRI NDVKPHPGGG IFYTAASGIW QTVWLEPVAS
AHITRLDMTP NLGDNTLRVK VQTAGAAGRS ARITVSSGGT VVGTATGAVS GEISVPVPNP
RLWTPEDPFL YDVKADLLDG SAVTDTVGSY TGMRSIGIAK VDNILRPVLN GKFVFQTGTL
DQGYWPDGIY TAPSDAALKY DLQAHKDLGF NMVRKHIKVE PQRWFYWADK LGLLVWQDMP
SMDTGKVPDG PARTQWEAEY RTIIDQHRSS PSVVMWVNQN EGWGQYDQAR IADEVKAQDP
SRLVNNMSGV NCCGSVDGGN GDVVDNHIYV GPGNTAPSAT RAAVLGEFGG LGYKAPGHEW
YPGGGFSYED QPSIAALNNR FVGLLDAIRI GQLPAGLSAS VYTEITDVEN EANGLLTYDR
QVVKVDTARV KAANQALIQA SRNPAPPVNL PTGQNKSLRV TTPGHTTKHL RHYDGLAFTE
VVNSGSPAVL KADATWKIVT GLANSNCYSF ESRNYPGEFL RHREFRVRRD ANDNSALFKA
DATWCAVAGT GGVRFTSANL PGSYLRHIDS EVWLATPGGG QPFDSPALFT EDTTWAVDAP
WAP
//
