ID A0A2N3HZV4_9BACT Unreviewed; 949 AA.
AC A0A2N3HZV4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Alpha-xylosidase {ECO:0000313|EMBL:PKQ63605.1};
GN ORFNames=BZG02_08535 {ECO:0000313|EMBL:PKQ63605.1};
OS Labilibaculum filiforme.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Marinilabiliales;
OC Marinifilaceae; Labilibaculum.
OX NCBI_TaxID=1940526 {ECO:0000313|EMBL:PKQ63605.1, ECO:0000313|Proteomes:UP000233535};
RN [1] {ECO:0000313|EMBL:PKQ63605.1, ECO:0000313|Proteomes:UP000233535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=59.16B {ECO:0000313|EMBL:PKQ63605.1,
RC ECO:0000313|Proteomes:UP000233535};
RX PubMed=29354105; DOI=10.3389/fmicb.2017.02614;
RA Vandieken V., Marshall I.P., Niemann H., Engelen B., Cypionka H.;
RT "Labilibaculum manganireducens gen. nov., sp. nov. and Labilibaculum
RT filiforme sp. nov., Novel Bacteroidetes Isolated from Subsurface Sediments
RT of the Baltic Sea.";
RL Front. Microbiol. 8:2614-2614(2017).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:PKQ63605.1}.
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DR EMBL; MVDD01000005; PKQ63605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3HZV4; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000233535; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06591; GH31_xylosidase_XylS; 1.
DR Gene3D; 2.60.120.380; -; 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 InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; GH.
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; IPR051816; Glycosyl_Hydrolase_31.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE; 1.
DR Pfam; PF17137; DUF5110; 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 Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS51820; PA14; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000233535};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..949
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014839827"
FT DOMAIN 227..367
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 949 AA; 109037 MW; 79266AFA993983E4 CRC64;
MKKIRIVALC GVLGMLALVT SCSQSKYKKL DNGIIVSLNK IENTDAALVK LEVVSDEIIR
VSSTPEKSFP SRESLVVLPQ LSKTDYTVEE DQNQIILSTA TIKAKVSLAT GEVAFYDLDG
NVLLKEADGV SKNFTPISAD GCKGYSFQQV FDSPEDEAFY GLGQHQSDEW NYKGKNEELY
QYNTKVSIPF VVSNKNYGLL WDNYSLTRFG NPNDYGQLSQ FKLYNKEGKE GALTATYTTG
KGEEFAKRDE ADIDYENLET VKKFPADFPF NNSKIVWEGE IEAKESGIYH FKLYYAGYTS
VSIGGKEVVG ERWRTAWNPN TYKFTVELKK GERVPVKLDW KPDGGISYIS LKALSPRPAE
EQGKLALWSE MGQELDYYFI HGDNMDKVIS GYRQLTGKAT ILPRWAYGFW QSRERYKTQK
EVVGTLAEFR KRKIPIDNIV IDWSYWEEDQ WGSHKFDASR FPDPQKMMDD IHAMNGHAMI
SVWPKFYTNT DNYKELDAKG FMYQQAVKDS VRDWIGKGHI GSFYDPYCKE ARQLFWNQMK
SNIYNFGMDA WWMDASEPDI VSNSSMEYRK KLMTPTAIGS STEFFNTYAL MNAKAIYNGQ
RSVDPNKRVF LLTRSGFAGL QRYSTATWSG DIGTRWEDMK AQITAGMNFA ISGIPYWTMD
IGGFCVEKRY EKAKEGSEDL KEWRELNTRW YQFGAFVPLF RAHGQYPYRE VYNIAPKSHK
AYQSILYYNK LRYRLMPYIY SLAGHVYFDD YTIMRALVMD FTKDTKVNDI DDQYMFGPSI
MVCPVSKFKA RERQVYLPEG SDWYDAYNGS LLKGGQTINA DAPYEKMPLF VKAGSILPVG
PEIEYTSQKL NAPIKLVIYT GADAQFELYE DEGLNFNYEK GKYSTISIKW SENDQKLTIG
ERKGEFEGMP QERIFTIVFA SETNKVDFNF DDHKGKEVKY NGKLVQVEL
//
