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Database: UniProt
Entry: L0KAU3_HALHC
LinkDB: L0KAU3_HALHC
Original site: L0KAU3_HALHC 
ID   L0KAU3_HALHC            Unreviewed;       726 AA.
AC   L0KAU3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:AGB41660.1};
GN   OrderedLocusNames=Halha_1723 {ECO:0000313|EMBL:AGB41660.1};
OS   Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Halobacteroides.
OX   NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB41660.1, ECO:0000313|Proteomes:UP000010880};
RN   [1] {ECO:0000313|Proteomes:UP000010880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC   {ECO:0000313|Proteomes:UP000010880};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Halobacteroides halobius DSM 5150.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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DR   EMBL; CP003359; AGB41660.1; -; Genomic_DNA.
DR   RefSeq; WP_015327376.1; NC_019978.1.
DR   AlphaFoldDB; L0KAU3; -.
DR   STRING; 748449.Halha_1723; -.
DR   KEGG; hhl:Halha_1723; -.
DR   PATRIC; fig|748449.3.peg.1676; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_009397_1_2_9; -.
DR   OrthoDB; 273314at2; -.
DR   Proteomes; UP000010880; 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   CDD; cd18832; GH43_GsAbnA-like; 1.
DR   Gene3D; 2.40.128.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR032291; Abn2_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF16369; GH43_C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010880}.
FT   DOMAIN          611..721
FT                   /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16369"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        467
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            414
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   726 AA;  80974 MW;  CF4DB3E50E620D4D CRC64;
     MNQKRKTLLS LVLSFLLVLS ITPVFVKAMS SGPVEQEQPE QSIETEQADS SGLVAHYTFN
     QELTDQTGNF EEGKVVGNRI NEEDGALISY GEGKRDQAAI FDGKSGIRLP DGLISSNVYS
     VALWVNPAKI TQFTTTFFGA QAKDQWISIV PNGPIGETML WSGEDWYDAP TGLKIPTDQW
     SHLTITVNQG EVKVYLNGQE RFSDSGFPDV FTNQKAKFAL GVNYWDAPFK GKLDDLRVYN
     TAIKAERVKK LAKGASKIKE PVENKTRVKL DQNSVAVHDP MIIKDKGTYY VFGSHLGAAK
     SDDLIHWKSI SNGFTVDNPI IPNPEQELKE ALEWPEPDAE STWAKSPIKL NGKYYLYFSS
     STWGAIRSAI GLAIAKNIEG PYEYQGLVIK SYKKGQENLE GVSHNPNVHP NAIDPQVFFD
     DQGKLWMTYG SYAGGIHILE MNSQTGKPYP NQGYGKRILG GNEAPIEGSY IQYNPKTEYY
     YLFASFGTLA ADGGYNIRVF RSKNPDGPYT DPQGHNSDYQ GTNELDFVKN NIDGHNWENV
     EPYGAKLIGN FLFQESKLGY LSPGHNSAIY DEVKDKMFIV FHSRFPGQGG RHQVRVHQML
     MNSRGWPVIT PHVYRGETAR KYSTEQVVGT YQYVNHGHDI QATFGNPGGD INLSKQIELN
     ADGSITGTVE GSWKMTGDYR VDITIDGETY HGAFLRQWDR GLKKNVMTFS ALSKQGVTIW
     GSEIPE
//
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