ID D3HX54_9BACT Unreviewed; 561 AA.
AC D3HX54;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EFC76214.1};
GN ORFNames=HMPREF0649_00836 {ECO:0000313|EMBL:EFC76214.1};
OS Segatella buccae D17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=575611 {ECO:0000313|EMBL:EFC76214.1, ECO:0000313|Proteomes:UP000005080};
RN [1] {ECO:0000313|EMBL:EFC76214.1, ECO:0000313|Proteomes:UP000005080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D17 {ECO:0000313|EMBL:EFC76214.1,
RC ECO:0000313|Proteomes:UP000005080};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., White A., Allen-Vercoe E., Strauss J., Crowley S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; GG739929; EFC76214.1; -; Genomic_DNA.
DR RefSeq; WP_004341400.1; NZ_GG739929.1.
DR AlphaFoldDB; D3HX54; -.
DR HOGENOM; CLU_016508_2_2_10; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000005080; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 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, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..561
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003046393"
FT DOMAIN 382..560
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 166
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 561 AA; 62511 MW; 384A837844B3EA53 CRC64;
MNKKTLLGAA LLLVSLAPRA QQATFSYFSY QGDEPRFRKQ IDTGREFFNP ILAGFYPDPS
ICRVGDTYYM VNSSFSFFPG VPLSTSKDLV HWTPAGHVLD RPSQVPLARQ KVSGGIFAPA
ISYNPKNKTF YMITTNVGAG NFYVKSKDPA KGWSEPIYLR KIDGIDPSFF FDKDGAGYIV
HNAPVDGGAD YEGQRAIRIF RFDTEGDSIV GDYKQIVRGG THVEKRPIWI EGPHLYRIGK
YYYLMCAEGG TGDWHSEVIF RSKSPMGPWE ENPDNPILTQ RTGLDPNRPD IVTSTGHADL
VQSKEGDWWA VFLGCRPYEA DYYNTGRDTY LLPVAWKNGW PVILDKEKAV PTVLAMKPWQ
QKMQKAVPVG AVATTGNFAY TDRFVGDRLD GRWMFLRNPS QFYSLGTDGL TINALPADIS
QREPLSAVFC RQQHTVFSAE TRVAFHPASD KQLAGLALLQ NEEYNFVMGK TRLNGRLAVV
LTRSERVNAV VASAFLDEAD ADKPLRLKID GHGRYYDFYY AVADGPWQLL ARGVDAVNLS
THRSGGFIGA CIGLYATAKG S
//