ID A0A1M6EAZ9_PSEXY Unreviewed; 1309 AA.
AC A0A1M6EAZ9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE SubName: Full=Fructan beta-fructosidase {ECO:0000313|EMBL:SHI82593.1};
GN ORFNames=SAMN02745725_01155 {ECO:0000313|EMBL:SHI82593.1};
OS Pseudobutyrivibrio xylanivorans DSM 14809.
OC Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC Lachnospiraceae; Pseudobutyrivibrio.
OX NCBI_TaxID=1123012 {ECO:0000313|EMBL:SHI82593.1, ECO:0000313|Proteomes:UP000184185};
RN [1] {ECO:0000313|EMBL:SHI82593.1, ECO:0000313|Proteomes:UP000184185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14809 {ECO:0000313|EMBL:SHI82593.1,
RC ECO:0000313|Proteomes:UP000184185};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902}.
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DR EMBL; FQYQ01000006; SHI82593.1; -; Genomic_DNA.
DR RefSeq; WP_072914114.1; NZ_FQYQ01000006.1.
DR OrthoDB; 9759709at2; -.
DR Proteomes; UP000184185; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IEA:TreeGrafter.
DR GO; GO:0005987; P:sucrose catabolic process; IEA:TreeGrafter.
DR CDD; cd18622; GH32_Inu-like; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.120.560; Exo-inulinase, domain 1; 3.
DR Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR42800; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR PANTHER; PTHR42800:SF1; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184185};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038828814"
FT TRANSMEM 1283..1304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 420..725
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 728..880
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
FT DOMAIN 904..971
FT /note="BIG2"
FT /evidence="ECO:0000259|Pfam:PF02368"
FT REGION 56..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1192
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 147393 MW; 7E77206FC9649525 CRC64;
MKRKRLVGFL CNLLSVSLLL CNVATNADIV FAEGSATNEI IVEEQNKDEN VEFTNPDEEI
IEEEKSDERD VNEEKKSDIT DLENENEGAQ TSDEEKFISD TEESEEDQIT DDKDDEDYID
NYKNNIGELS YSGDGNWEYT EDGLMSDALG KGDCFAFSKT HGKNFVYSTD IKFLENQLAA
ALLFRSNGTA DNKESYVVNL DASNHKCKFF RWQRNDALQL IDEKSITATS EETYTLKVVA
CDSWILYFVN DELVASLGDY YLQPGDLGQD TFIDEGVFGL LNWNSKVIFQ NTYYRELNNY
FSPLLKDISV KSDNGTISDK ARFLSTEPMM LQYVNNDASE VKIELEKMCP DASIEIKNED
GDLFSVGESI PIETGINYIT VKSTIKDDDG FDASVVYRLN IHRFKNDVEY YNEVYRDQYH
YSVKEGWAND PNGLVYYKGT YHMFYQFFDD IKWGPMHWAH ATSKDLLHWQ EEPIAFYPDA
NGAMFSGCIV VDDNNTSGLF DSNEGGLVAL ITADGNGQRI KLAYSEDEGR TWKKLDKVAL
DWSNDPLHSR DFRDPKVFRW ENKWFMVIAG GPLRIYSSDN LIDWTCESTY GDLHTECPDM
YPVKASDGTL KWVLSRGGRF YKVGDFRNLD GCWTFIPDDE YKDSDGIMNF GRDSYAAMTY
YIQDFGTAAN PDIPEIVELN WMNTWDDYCN QIASKVGQDF NGTFNLNLKL GLEKTDAGYA
LTQTPINEYK KLRETTNKLH IKNLKLKDSA DTLKDFNGDT YEIIARFKPA KNATKVGFKL
RKGSNEETIV AYDFNDQKLY IDRSNSGVII SNKFSEVCSQ NMSLNGDGSL DLHIFVDKAS
VEVFSADNKV CGAAQIFANP FSQGIEVFAE SGEINADIDI YPIKSIWNDK KEVKDVYAIS
SMFPSKTRMN CGEKTKIDAY ILPVNANQKI NWTIKSGEGV IQLSDDGKVE AIKKGTAVVS
ATSEENPELS KEFTIEVYEN NFKTNVKDFV NLSGNWTVDD ETLTVSNVCQ NDYYMVKDKI
NGDYTMKTKI NFTKGLINIF LVSPNMNPLE GEGGYTIQFA PDNKVIRFFR FGRDDMFRGQ
LKAPIGDGKY HNLEIKKKNN NISVFVDDVN SLDYTLEDAN DLEEGYVGLG LWDGELNVQT
FYVDSKDTEK PAEDKPATPS TNDNKLDISA SNSGSSSGSS NSNRASNTTS NNGQTQVKIA
DEPVAQALPK QEATNKISTK NSSKKPSEKE EQAATEDIST KDNSFEEKAS EEIQDETVPK
AAVETENDSA TESIAEESTS NNAVIAILCV LGILLACGLV ILMIRKKKM
//
