ID A0A096AY43_9BACT Unreviewed; 1292 AA.
AC A0A096AY43;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Alpha-xylosidase {ECO:0000313|EMBL:KGF35477.1};
GN ORFNames=HMPREF2137_04820 {ECO:0000313|EMBL:KGF35477.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF35477.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF35477.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF35477.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF35477.1}.
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DR EMBL; JRNN01000042; KGF35477.1; -; Genomic_DNA.
DR RefSeq; WP_036872330.1; NZ_JRNN01000042.1.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000029556; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1292
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001925223"
FT DOMAIN 872..954
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 943..1072
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1292 AA; 145393 MW; 8FD88C3E7DBA3F1A CRC64;
MKQSFSLLAL TTFTSLSVWM VNPAVASNHA MMNRAGVTSA VGVGQQSPAQ ALVTDARMLN
DHAVVFTLAT NQQVVVDFYG PNIFRLYQDS IGVPMHNPQA KPQADILVAQ SRRAVGTVDL
KLQGDSYLLT TSSLQVALSK QQGAMALTDL RTGQVVVRTL AAPIIEKDKV KLQLTCRPDE
YFYGGGVQNG RFSHKGKKIA IENTNNWVDG GVASPTPYYW STKGYGVMWH TFRPGIYDFG
ATDRSKVLLQ HDTRHLDCFF MVDSAPTALL NDFYQLTGHP VLLPKFGFYE GHLNAYNRDY
WKEVKKGRGV MTFEDGKEYT ESQKDNGGVK ESLNGEKNNY LFSARAAIDR YVKHDMPLGW
FLPNDGYGAG YGQTATLDGN IANLKMFGDY ARSKGVEIGL WTQSDLHPKD GVEALLQRDI
IKEVRDAGVR VLKTDVAWVG WGYSFGLNGV ADVGTIMPRY GDNARPFIIT LDGWAGTQRY
AGVWTGDQTG GDWEYIRFHI PTFIGSGLSG QPNVTSDVDG IFGGRNVPVN VREFQWKTFT
PMALNMDGWG ANPKYPFILG GKSVALNRWS LKLKSQLIPY IYTTAHDAVT GKPMMRPMFM
EERNDYTLGN RTQYQYMFGD AFLVAPVYKD THADKEGNDV RDYIYLPHGT WIDYFTGQRY
TGGRIINQFD APLWKLPLFV KADAIIPYTH ANNNPSEIRR DYRAYEIYAM NGCVGHEYDD
DGKTQAYLKG EGVNTKISTQ VKKDMLTVQV EKTTGGYQGF EPEKQTDFKL NVTRMPKKLW
TKVGNRKTKL KQVFSQKEFE QGENVWFYNE RPDLNQWVKA GEESVGEVIK NPQVYVRLAK
NNVTEHATEL VVKGFCFQPA EALLHQHGPL AAPTFNQQRS KAQAYQLTPA WNEVKGADYY
ELEFDGQIYS TLRTPQCTID DLQPLTSYHF RVRAVNADGK SDWLSFTLST VSDPFEWAVK
ELRAQTTVPA QTGEGTVKLF DRDVKTIWHT AWDNNKVLPF DMIVDLRAVH QLDRLCYVPR
ADAGNGTILK GTWALSADRQ TWTDPTAFTW QRNADEKCIA FTARPKARYI KLRFEEAVGG
FGSGAEMYVF RKPNTEGEIQ GDINRDKRID ENDLTSYMNY TGLRRGDADY DYVSIGDINR
NGLIDAYDIS CVGVELDGGA SQRNDQVRGS LELIAPKTFK AGDDIEIQVV GKNLHFVNAL
SFALPYNADE LEYRGVTLQG MKEMVNLTYD RLHTNGQKAL YPTFVNRGNN FLLDEGDPKL
FIIKFHAKKS GKLNLKMRDG MLVDRNLGVS NF
//
