ID H1YFR6_9SPHI Unreviewed; 560 AA.
AC H1YFR6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:EHQ25307.1};
GN ORFNames=Mucpa_1139 {ECO:0000313|EMBL:EHQ25307.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ25307.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ25307.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ25307.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) 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; CM001403; EHQ25307.1; -; Genomic_DNA.
DR RefSeq; WP_008505003.1; NZ_CM001403.1.
DR AlphaFoldDB; H1YFR6; -.
DR STRING; 714943.Mucpa_1139; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_2_2_10; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000002774; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000002774}.
FT DOMAIN 364..551
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 147
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 560 AA; 62898 MW; 38036BA8E6CF1C1A CRC64;
MKIKIIVINT LIIGCLLKGI YAQAQSIKLV NPILSGFYPD PSIVKVGADY YLVNSTFAYF
PGLPLFHSKD LKNWKQVANI IDRDSQMNFI GDRMTRGLFA PGISYNKGTF YVTCTNIDHR
GNFVVTAANP AGPWSNPVWL PEVKGIDPSI FFDADKAYIV YNSDAPDNKP AYSGHRTIRI
YELDIQNLKI TGEEKILVNG GVDISKKPVW IEGPHILKRN DWYYLYAAEG GTSVNHSEVV
FRSKRVDGPY VPYEHNPILT QRDLPEDRKY PVTSTGHAQF VEGPDNKTYA VFLGVRPYTG
DYYNTGRETF IAPVEWKNDW PVINPGKGEI KYEYTAAYKE VKLGKALPQS GNFSYTLTFD
KGIDASLLFL RSRDTASYSF NKQAGLILKL KPETCMGTGT PSFVGKRQQH LICTAETELT
FSPQKDNEKA GLVIFQDEKH FYFLGKCITN GKNVLQLYKS KDDKKTMEVI AEVPLTPNAK
PVQLRIDADG ENYSCYYAVE QGKWILLKDK LDAKFLSTHE AGGFIGCIFG LYATSSGETG
SNTASFKYLR YSGNDQVYKQ
//
